+ |
CDK1 | up-regulates activity
phosphorylation
|
FMNL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273555 |
Ser1016 |
MEQQDPKsPSHKSKR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
29930204 |
In this study we have identified the formin FMNL2 as a novel substrate for CDK1 that plays a role in maintaining adhesion complexes and facilitates cell cycle–dependent changes in adhesion complexes. Knockdown of FMNL2 or expression of a nonphosphorylatable S1016A mutant resulted in the loss of adhesion complexes and stress fibers within the cell body, with peripheral structures being maintained. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | up-regulates activity
phosphorylation
|
FMNL2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273796 |
Ser1072 |
ARTAKRGsRFFCEPV |
in vitro |
|
pmid |
sentence |
26256210 |
PKCα associates with and phosphorylates FMNL2 at S1072 within its Diaphanous autoregulatory region, leading to the release of formin autoinhibition. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
FMNL2 | up-regulates activity
binding
|
PLK1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273614 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
19386263 |
Phosphorylation of hCenexin1 at S796 is critical for the hCenexin1-Plk1 interaction.Here we show that a splice variant of hODF2 called hCenexin1, but not hODF2 itself, efficiently localizes to somatic centrosomes via a variant-specific C-terminal extension and recruits Plk1 through a Cdc2-dependent phospho-S796 motif within the extension. This interaction and Plk1 activity were important for proper recruitment of pericentrin and gamma-tubulin, and, ultimately, for formation of normal bipolar spindles. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |