| + |
ROCK1 | up-regulates 
phosphorylation
|
RND3 |
0.736 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134703 |
Ser11 |
RRASQKLsSKSIMDP |
Homo sapiens |
|
| pmid |
sentence |
| 15775972 |
We show that rock phosphorylates endogenous rhoe at serine 11 upon cell stimulation with platelet-derived growth factor. Phosphorylation has no effect on rhoe binding to rock i, but instead increases rhoe protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
FHOD1 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160544 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160548 |
Ser1137 |
RSRGNRKsLRRTLKS |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160552 |
Thr1141 |
NRKSLRRtLKSGLGD |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates 
phosphorylation
|
ARHGAP35 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182849 |
Ser1150 |
LERGRKVsIVSKPVL |
Homo sapiens |
|
| pmid |
sentence |
| 19103606 |
Rho-kinase, an effector of rhoa, phosphorylated p190a rhogap at ser(1150) and attenuated p190a rhogap activity in cos7 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182853 |
Ser1236 |
PKPKPRPsITKATWE |
Homo sapiens |
|
| pmid |
sentence |
| 19103606 |
Here we show that rho-kinase, an effector of rhoa, phosphorylated p190a rhogap at ser1150 and attenuated p190a rhogap activity in cos7 cells |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
ARHGAP35 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276177 |
Ser1150 |
LERGRKVsIVSKPVL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276176 |
Ser1236 |
PKPKPRPsITKATWE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276178 |
Thr1226 |
LRSLRRNtKKPKPKP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
GFAP |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100181 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100188 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100192 |
Thr7 |
tSAARRSY |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates
phosphorylation
|
PFN1 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196820 |
Ser138 |
MASHLRRsQY |
Homo sapiens |
|
| pmid |
sentence |
| 22479341 |
We previously identified pfn1 as a huntingtin aggregation inhibitor, and others have implicated it as a tumor-suppressor. Rho-associated kinase (rock) directly phosphorylates pfn1 at ser-137 to prevent its binding to polyproline sequences. This negatively regulates its anti-aggregation activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
SOX9 |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162643 |
Ser181 |
YQPRRRKsVKNGQAE |
Homo sapiens |
|
| pmid |
sentence |
| 20039424 |
Rho kinase-dependent activation of sox9 in chondrocytes. In vitro, rock directly phosphorylated sox9 at ser(181), and the overexpression of rock or the activation of the rhoa pathway in sw1353 chondrosarcoma cells increased sox9(ser181) phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MYL12A |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263073 |
Ser19 |
KRPQRATsNVFAMFD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12185584 |
Phosphorylation of myosin II regulatory light chain (MRLC) is important for cell motility and cytokinesis in nonmuscle cells. Although the regulation of monophosphorylated MRLC at serine 19 throughout the cell cycle was examined in detail, MRLC diphosphorylation at both threonine 18 and serine 19 is still unclear. Here we found that Rho-kinase has an activity for MRLC diphosphorylation in nonmuscle cells using sequential column chromatographies. we showed that the inhibition of Rho-kinase reduced diphosphorylated MRLC in the center of cells even in the presence of phosphatase inhibitor, suggesting that Rho-kinase directly diphosphorylates MRLC (red arrow in Figure 6). Taken together, we propose a model of diphosphorylation of MRLC through dual pathways of both the direct phosphorylation and the inhibition of myosin phosphatase by Rho-kinase (Figure 6). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263074 |
Thr18 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Phosphorylation of myosin II regulatory light chain (MRLC) is important for cell motility and cytokinesis in nonmuscle cells. Although the regulation of monophosphorylated MRLC at serine 19 throughout the cell cycle was examined in detail, MRLC diphosphorylation at both threonine 18 and serine 19 is still unclear. Here we found that Rho-kinase has an activity for MRLC diphosphorylation in nonmuscle cells using sequential column chromatographies. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MYL9 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260307 |
Ser20 |
KRPQRATsNVFAMFD |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260308 |
Thr19 |
KKRPQRAtSNVFAMF |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ROCK1 | up-regulates
phosphorylation
|
MYL9 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43031 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Rho-kinase phosphorylates the mlc of intact myosin and activates its mgatpase activity in a gtp_?Rho-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
ROCK1 | up-regulates
phosphorylation
|
MYL12B |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91542 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Here we found that rho-kinase has an activity for mrlc diphosphorylation at both threonine 18 and serine 19 in nonmuscle cells using sequential column chromatographies. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91546 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Here we found that rho-kinase has an activity for mrlc diphosphorylation at both threonine 18 and serine 19 in nonmuscle cells using sequential column chromatographies. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
PTEN |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134851 |
Ser229 |
VKIYSSNsGPTRRED |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134855 |
Thr232 |
YSSNSGPtRREDKFM |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Hindbrain |
| + |
ROCK1 | up-regulates
phosphorylation
|
MAPK8IP3 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134580 |
Ser314 |
RAREKRDsRNMEVQV |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134584 |
Ser364 |
TRLDRTGsSPTQGIV |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134588 |
Ser365 |
RLDRTGSsPTQGIVN |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
KCNK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176025 |
Ser336 |
IPRDLSTsDTCVEQS |
Homo sapiens |
|
| pmid |
sentence |
| 21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
ARHGAP24 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249309 |
Ser391 |
RSSMNNGsPTALSGS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249304 |
Ser402 |
LSGSKTNsPKNSVHK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249306 |
Ser413 |
SVHKLDVsRSPPLMV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249307 |
Ser415 |
HKLDVSRsPPLMVKK |
Homo sapiens |
|
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDS‚‚PAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573‚‚577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249305 |
Ser437 |
SGIVTNGsFSSSNAE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249302 |
Ser573 |
ENSNSCRsSTTTCPE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249303 |
Ser574 |
NSNSCRSsTTTCPEQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249310 |
Thr452 |
GLEKTQTtPNGSLQA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249299 |
Thr575 |
SNSCRSStTTCPEQD |
Homo sapiens |
|
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249300 |
Thr576 |
NSCRSSTtTCPEQDF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249301 |
Thr577 |
SCRSSTTtCPEQDFF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176029 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
| pmid |
sentence |
| 21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
DNM1L |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262549 |
Ser637 |
VPVARKLsAREQRDC |
Mus musculus |
|
| pmid |
sentence |
| 31063459 |
We have also previously reported that ROCK1-mediated Drp1S600 phosphorylation resulted in enhanced mitochondrial fission in podocytes |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
VIM |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248998 |
Ser72 |
SSAVRLRsSVPGVRL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9565595 |
We found that vimentin, the most widely expressed intermediate filament protein, served as an excellent substrate for Rho-associated kinase (Rho-kinase) and that vimentin phosphorylated by Rho-kinase lost its ability to form filaments in vitro. Two amino-terminal sites on vimentin, Ser38 and Ser71, were identified as the major phosphorylation sites for Rho-kinase, and Ser71 was the most favored and unique phosphorylation site for Rho-kinase in vitro. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 |
phosphorylation
|
DES |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249032 |
Thr17 |
RVSSYRRtFGGAPGF |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249031 |
Thr76 |
LRASRLGtTRTPSSY |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249033 |
Thr77 |
RASRLGTtRTPSSYG |
Homo sapiens |
SAOS-2 Cell |
| pmid |
sentence |
| 10574968 |
We developed antibodies specifically recognizing the kinase-dependent phosphorylation of desmin at Thr-16, Thr-75, and Thr-76. With these antibodies, phosphorylation of desmin was observed specifically at the cleavage furrow in late mitotic Saos-2 cells. We then found that treatment of the interphase cells with calyculin A revealed phosphorylation at all the three sites of desmin |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
DES |
0.32 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100177 |
Thr17 |
RVSSYRRtFGGAPGF |
in vitro |
|
| pmid |
sentence |
| 12686604 |
The sites phosphorylated by Aurora-B; Thr-7/Ser-13/Ser-38 of GFAP, and Thr-16 of desmin are common with those related to Rho-associated kinase (Rho-kinase), which has been reported to phosphorylate GFAP and desmin at cleavage furrow during cytokinesis. Rho-kinase was found to phosphorylate desmin at Thr-16, Thr-75, and Thr-76 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK1 | up-regulates
phosphorylation
|
ADD1 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66992 |
Thr445 |
QKQQREKtRWLNSGR |
Homo sapiens |
|
| pmid |
sentence |
| 10209029 |
Rho-associated kinase (rho- kinase), which is activated by the small guanosine triphosphatase rho, phosphorylates alpha-adducin and thereby enhances the f-actin-binding activity of alpha-adducin in vitro. Here we identified the sites of phosphorylation of alpha-adducin by rho-kinase as thr445 and thr480 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66996 |
Thr480 |
TKEDGHRtSTSAVPN |
Homo sapiens |
|
| pmid |
sentence |
| 10209029 |
Rho-associated kinase (rho- kinase), which is activated by the small guanosine triphosphatase rho, phosphorylates alpha-adducin and thereby enhances the f-actin-binding activity of alpha-adducin in vitro. Here we identified the sites of phosphorylation of alpha-adducin by rho-kinase as thr445 and thr480 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
ROCK1 | up-regulates
phosphorylation
|
LIMK2 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82755 |
Thr505 |
NDRKKRYtVVGNPYW |
Homo sapiens |
|
| pmid |
sentence |
| 11018042 |
Specific activation of lim kinase 2 via phosphorylation of threonine 505 by rock, a rho-dependent protein kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
LIMK1 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74569 |
Thr508 |
PDRKKRYtVVGNPYW |
Homo sapiens |
|
| pmid |
sentence |
| 10652353 |
Rho-associated kinase rock activates lim-kinase 1 by phosphorylation at threonine 508 within the activation loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
LIMK2 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249053 |
Thr526 |
NGKSYDEtVDIFSFG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11018042 |
Specific Activation of LIM kinase 2 via Phosphorylation of Threonine 505 by ROCK, a Rho-dependent Protein Kinase |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 |
phosphorylation
|
DPYSL2 |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249042 |
Thr555 |
DNIPRRTtQRIVAPP |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10818093 |
We produced an antibody that specifically recognizes CRMP-2 phosphorylated at Thr-555. Using this antibody, we found that Rho-kinase phosphorylated CRMP-2 downstream of Rho in COS7 cells. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MSN |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249014 |
Thr558 |
LGRDKYKtLRQIRQG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9856983 |
Rho-associated kinase (Rho-kinase), which is activated by the small GTPase Rho, phosphorylates moesin at Thr558 in vitro. Here, using a site- and phosphorylation state-specific antibody, we found that the expression of dominant active RhoA in COS7 cells induced moesin phosphorylation and the formation of microvilli-like structures at apical membranes where the Thr558-phosphorylated moesin accumulated, whereas the expression of dominant negative Rho-kinase inhibited both of these processes. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
RDX |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248994 |
Thr564 |
AGRDKYKtLRQIRQG |
Mus musculus |
Swiss-3T3 Cell |
| pmid |
sentence |
| 9456324 |
A peak of the phosphopeptide, in which only T573 was phosphorylated, was not detected. Quantitative analyses revealed that _100% of T564, but at most _40% of T573, was phosphorylated when C-rad was incubated with Rho-Kc for 1 h. Then we concluded that the major and primary phosphorylation site of radixin by Rho-kinase was T564 and referred to the Rho-Kcphosphorylated C-rad as T564-phosphorylated C-rad. | In this study, we found that the T564 phosphorylation of radixin markedly suppressed its head-to-tail association. This suggests that the T564-phosphorylation of radixin (and probably also the phosphorylation of ezrin T567 and moesin T558) keeps them open and active. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ROCK1 | up-regulates
phosphorylation
|
EZR |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185567 |
Thr567 |
QGRDKYKtLRQIRQG |
Homo sapiens |
|
| pmid |
sentence |
| 19386264 |
Activation of ezrin is mediated by initial pip2 binding and subsequent phosphorylation of threonine 567. We performed an in vitro kinase assay with 80 selected kinases on an ezrin peptide containing the t567 phosphorylation site (figure 3a). In this screen, we identified the mst and rock kinases as the most potent kinases for the ezrin peptide |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 |
phosphorylation
|
RDX |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248995 |
Thr573 |
RQIRQGNtKQRIDEF |
in vitro |
|
| pmid |
sentence |
| 9456324 |
A peak of the phosphopeptide, in which only T573 was phosphorylated, was not detected. Quantitative analyses revealed that _100% of T564, but at most _40% of T573, was phosphorylated when C-rad was incubated with Rho-Kc for 1 h. Then we concluded that the major and primary phosphorylation site of radixin by Rho-kinase was T564 and referred to the Rho-Kcphosphorylated C-rad as T564-phosphorylated C-rad. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates
phosphorylation
|
PPP1R12B |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198812 |
Thr646 |
ARQTRRStQGVTLTD |
Homo sapiens |
|
| pmid |
sentence |
| 22937917 |
Phosphorylation of ppp1r12b on threonine 646 by rho kinase inhibits the activity of the pp1c-ppp1r12b complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
PPP1R12A |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42354 |
Thr696 |
ARQSRRStQGVTLTD |
Homo sapiens |
|
| pmid |
sentence |
| 8662509 |
Rho-associated kinase (rho-kinase) phosphorylated mbs and consequently inactivated myosin phosphatase. Rho appears to inhibit myosin phosphatase through the action of rho-kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
PPP1R12A |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249034 |
Thr853 |
PREKRRStGVSFWTQ |
Mus musculus |
|
| pmid |
sentence |
| 10601309 |
Phosphorylation by Rho-kinase inhibited MP activity and this reflected a decrease in V(max). Activity of MP with different substrates also was inhibited by phosphorylation. Two major sites of phosphorylation on MYPT1 were Thr(695) and Thr(850). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
N-(6-fluoro-1H-indazol-5-yl)-6-methyl-2-oxo-4-[4-(trifluoromethyl)phenyl]-3,4-dihydro-1H-pyridine-5-carboxamide | down-regulates activity
chemical inhibition
|
ROCK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262229 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19740074 |
We also observed that several ROCK (Rho kinase) inhibitors such as Y-27632 and H-1152, suppressed LRRK2 with similar potency to which they inhibited ROCK2. In contrast, GSK429286A, a selective ROCK inhibitor, did not significantly inhibit LRRK2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
ARHGAP24 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148262 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16862148 |
Rock phosphorylates filgap, and this phosphorylation stimulates its racgap activity and is a requirement for filgap-mediated bleb formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAC1 | up-regulates activity
binding
|
ROCK1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258972 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27571105 |
Although there are other activators of PCP, Wnt5a can activate the PCP pathway by forming a complex with Fzd and Ror2 receptors, activating DVL, which in turn activates Rho-family small GTPases, including RhoA and Rac, and their downstream effectors, Rho-associated protein kinase (ROCK), the actin-binding protein, Filamin A and c-Jun N-terminal protein kinase (JNK) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MAPK8 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123717 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15068801 |
Instead, we found that rock activates jnk, which then phosphorylates c-jun and atf2 when bound to the c-jun promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis |
| + |
ROCK1 | up-regulates 
|
Membrane_blebbing |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106549 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Activation of rock i by caspase-3 seems to be responsible for bleb formation in apoptotic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258975 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19279717 |
To date it is not clear whether any genes are transcribed downstream of these two GTPases for non-canonical signaling. The prevailing dogma remains that their primary roles are indeed solely for cytoskeletal modulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Y-27632 | down-regulates
chemical inhibition
|
ROCK1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207890 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
binding
|
MYLK |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106552 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Rock proteins are known to regulate mlc-phosphorylation, and apoptotic cells exhibit a gradual increase in levels of phosphorylated mlc concomitant with rock i cleavage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RHOA | up-regulates activity
binding
|
ROCK1 |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196740 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25010901 |
Rho-associated coiled-coil containing kinases (ROCK) were originally identified as effectors of the RhoA small GTPase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199542 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23151663 |
Planar cell polarity (pcp) signalling triggers activation of the small gtpases rhoa and rac1, which in turn activate rho kinase (rock) and jun-n-terminal kinase (jnk), respectively, leading to actin polymerization and microtubule stabilization. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis |
| + |
ROCK1 | up-regulates quantity by expression
transcriptional regulation
|
LPP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198118 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22886954 |
Inactivation of rho kinase (rok) with rok inhibitors significantly inhibited lpp mrna expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
ROCK1 | up-regulates
|
Brown_adipogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198840 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22944199 |
Other g protein-mediated pathways are the planar cell polarity (pcp) pathway (shown in blue) leading to the activation of rac/rho, c-jun n-terminal kinase (jnk), and/or rho-associated kinase (rock). Jnk can induce jun, which, together with fos, forms the ap-1 early response transcription factor. Both pcp pathways have been implicated in cytoskeletal rearrangements |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| Pathways: | WNT Signaling and Myogenesis |
| + |
Caspase 3 complex | up-regulates
cleavage
|
ROCK1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256460 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Rock i is cleaved by casp3 at a conserved detd1113/g sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
MPRIP |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157593 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17761936 |
Enhanced rho kinase activity induces endothelial barrier dysfunction by a contractile mechanism via inactivation of myosin phosphatase (mp).. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DRAM2 | up-regulates quantity by expression
transcriptional regulation
|
ROCK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30755245 |
Here, we show that DRAM2 may act as an oncogenic regulator in non-small cell lung cancer (NSCLC). Furthermore, DRAM2 overexpression increased the expression of proteins RAC1, RHOA, RHOC, ROCK1, and decreased RHOB expression, all of which are cell migration factors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CASP3 | up-regulates
cleavage
|
ROCK1 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Rock i is cleaved by casp3 at a conserved detd1113/g sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
transcriptional regulation
|
Satellite_cells_self-renewal |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255850 |
|
|
|
|
| pmid |
sentence |
| 23290138 |
FN in the satellite cell niche is required for the maintenance of the overall satellite cell pool during muscle regeneration. Moreover, FN is necessary to potentiate Wnt7a signaling through the Fzd7/Scd4 receptor complex, which controls the regulation of satellite stem cell numbers |
|
| Publications: |
1 |
| Tissue: |
Skeletal Muscle |
3.0
ROCK1
- 
- 