| + |
MARK3 | up-regulates activity
phosphorylation
|
ARHGEF2 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277368 |
Ser151 |
LSLAKSVsTTNIAGH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 29089450 |
Rho-Rac guanine nucleotide exchange factor 2 (ARHGEF2), which activates Ras homolog family member A (RHOA), is anchored to the microtubule network and sequestered in an inhibited state through binding to dynein light chain Tctex-1 type 1 (DYNLT1). We showed in mammalian cells that liver kinase B1 (LKB1) activated the microtubule affinity-regulating kinase 3 (MARK3), which in turn phosphorylated ARHGEF2 at Ser151 This modification disrupted the interaction between ARHGEF2 and DYNLT1 by generating a 14-3-3 binding site in ARHGEF2, thus causing ARHGEF2 to dissociate from microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARK2 | down-regulates
phosphorylation
|
ARHGEF2 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177096 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 22072711 |
We also show that par1b-induced serine 885/serine 959 phosphorylation inhibits rhoa-specific gef activity of gef-h1. As a consequence, gef-h1 phosphorylated on both of the serine residues loses the ability to stimulate rhoa and thereby fails to induce rhoa-dependent stress fiber formation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177100 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
|
| pmid |
sentence |
| 22072711 |
We also show that par1b-induced serine 885/serine 959 phosphorylation inhibits rhoa-specific gef activity of gef-h1. As a consequence, gef-h1 phosphorylated on both of the serine residues loses the ability to stimulate rhoa and thereby fails to induce rhoa-dependent stress fiber formation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
ARHGEF2 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187573 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 19667072 |
We identify gef-h1 as a binding target and substrate for p21-activated kinase 1 (pak1), we show that phosphorylation of gef-h1 at ser(885) by pak1 induces 14-3-3 binding to the exchange factor and relocation of 14-3-3 to microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
ARHGEF2 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122191 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 14970201 |
Here we identify a region in the carboxyl terminus of gef-h1 that is important for suppression of its guanine nucleotide exchange activity by microtubules. This portion of the protein includes a coiled-coil motif, a proline-rich motif that may interact with src homology 3 domain-containing proteins, and a potential binding site for 14-3-3 proteins. We show that phosphorylation of gef-h1 at ser(885) by pak1 induces 14-3-3 binding to the exchange factor and relocation of 14-3-3 to microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKB | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276062 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17488622 |
The mitotic kinases Aurora A/B and Cdk1/Cyclin B phosphorylate GEF-H1, thereby inhibiting GEF-H1 catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276061 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17488622 |
The mitotic kinases Aurora A/B and Cdk1/Cyclin B phosphorylate GEF-H1, thereby inhibiting GEF-H1 catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinB/CDK1 | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276060 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17488622 |
The mitotic kinases Aurora A/B and Cdk1/Cyclin B phosphorylate GEF-H1, thereby inhibiting GEF-H1 catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
ARHGEF2 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279359 |
Thr103 |
AALLKNNtALQSVSL |
Homo sapiens |
|
| pmid |
sentence |
| 28652571 |
In this study, we found that CaMKI phosphorylated GEF-H1 at Thr103, which is located close to the C1 domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | up-regulates
phosphorylation
|
ARHGEF2 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184469 |
Thr679 |
PGVELLLtPREPALP |
Homo sapiens |
|
| pmid |
sentence |
| 19261619 |
Importantly tnf-alpha enhanced the erk pathway-dependent phosphorylation of thr-678 of gef-h1 that was key for activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
MAPK3 | up-regulates
phosphorylation
|
ARHGEF2 |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160420 |
Thr679 |
PGVELLLtPREPALP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18211802 |
Activates rhoa and as a result regulates actin assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
ARHGEF2 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277478 |
Tyr198 |
IDEAEVIySELMSDF |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31420453 |
Src activates GEF-H1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R9B | up-regulates activity
binding
|
ARHGEF2 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269176 |
|
|
Mus musculus |
Neuro-2a Cell |
| pmid |
sentence |
| 15996550 |
The Rho Family GEF Lfc Interacts with Neurabin and Spinophilin. Neurabin and spinophilin are homologous protein phosphatase 1 and actin binding proteins that regulate dendritic spine function. The results obtained in the present study suggest a mechanism by which neurabin or spinophilin contributes to the organization of the F-actin cytoskeleton in dendritic spines, and in turn to the regulation of spine morphology, via the activity-dependent recruitment of the Rho-specific GEF Lfc |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PAK4 | down-regulates activity
phosphorylation
|
ARHGEF2 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279245 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23125951 |
PAK4 specifically phosphorylates GefH1, and this is thought to inhibit its ability to activate Rho, consequently inhibiting stress fiber formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK9 | up-regulates activity
phosphorylation
|
ARHGEF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279638 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33500736 |
The phosphorylation of ARHGEF2 by NEK9 is the key step of this process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates
phosphorylation
|
ARHGEF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270007 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18211802 |
Activates rhoa and as a result regulates actin assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARHGEF2 | up-regulates activity
guanine nucleotide exchange factor
|
RHOA |
0.806 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260529 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32203420 |
We therefore developed a screening-compatible live-cell imaging assay, using FRET-based biosensors for the prototype GTPases RHOA, RAC1 and CDC4215,19,20 (Extended Data Fig. 2 and Supplementary Note 1)|We found catalytic activities for 45/75 RhoGEFs and 48/63 RhoGAPs| Our data thus not only reveal extensive promiscuity among regulators, but also that the inactivating RhoGAPs are less selective than the activating RhoGEFs (p-value=0.02)(Supplementary Table 2). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1R9A | up-regulates activity
binding
|
ARHGEF2 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269177 |
|
|
Mus musculus |
Neuro-2a Cell |
| pmid |
sentence |
| 15996550 |
The Rho Family GEF Lfc Interacts with Neurabin and Spinophilin. Neurabin and spinophilin are homologous protein phosphatase 1 and actin binding proteins that regulate dendritic spine function. The results obtained in the present study suggest a mechanism by which neurabin or spinophilin contributes to the organization of the F-actin cytoskeleton in dendritic spines, and in turn to the regulation of spine morphology, via the activity-dependent recruitment of the Rho-specific GEF Lfc |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DYNLT1 | down-regulates activity
binding
|
ARHGEF2 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277369 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 29089450 |
Rho-Rac guanine nucleotide exchange factor 2 (ARHGEF2), which activates Ras homolog family member A (RHOA), is anchored to the microtubule network and sequestered in an inhibited state through binding to dynein light chain Tctex-1 type 1 (DYNLT1). We showed in mammalian cells that liver kinase B1 (LKB1) activated the microtubule affinity-regulating kinase 3 (MARK3), which in turn phosphorylated ARHGEF2 at Ser151 This modification disrupted the interaction between ARHGEF2 and DYNLT1 by generating a 14-3-3 binding site in ARHGEF2, thus causing ARHGEF2 to dissociate from microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
ARHGEF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270138 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18211802 |
Activates rhoa and as a result regulates actin assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |