| + |
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 |
| + |
PAK2 | up-regulates activity
phosphorylation
|
MYL12A |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263020 |
Ser19 |
KRPQRATsNVFAMFD |
in vitro |
|
| pmid |
sentence |
| 10047984 |
In this study we report that gamma-PAK, which is activated by the GTP-binding proteins Cdc42 and Rac, catalyses phosphorylation of intact non-muscle myosin II and isolated recombinant RLC. Phosphopeptide maps and phosphoamino acid analysis revealed that gamma-PAK phosphorylates Ser-19 but does not phosphorylate Thr-18.Taken together, these data suggest that myosin II activation by the p21-activated family of kinases may be physiologically important in regulating cytoskeletal organization. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
DAPK1 | up-regulates activity
phosphorylation
|
MYL12A |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262842 |
Ser19 |
KRPQRATsNVFAMFD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11485996 |
DAPK Phosphorylates Myosin II RLC in Vitro and in Vivo. Together these results show that similar to the conventional MLCKs, Ser-19 is the primary RLC residue phosphorylated by DAPK and that phosphorylation of Thr-18 is also possible. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262843 |
Thr18 |
KKRPQRAtSNVFAMF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11485996 |
DAPK Phosphorylates Myosin II RLC in Vitro and in Vivo. Together these results show that similar to the conventional MLCKs, Ser-19 is the primary RLC residue phosphorylated by DAPK and that phosphorylation of Thr-18 is also possible. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
MYL12A
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