+ |
CyclinA2/CDK2 | down-regulates activity
phosphorylation
|
CEP76 |
0.305 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262603 |
Ser83 |
VEQELPSsPKQPICF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27065328 |
Cep76 is phosphorylated by cyclin A/CDK2 at a single site S83. These data suggest that the phosphomimetic mutant is functional and that phosphorylation at S83 is critical for Cep76 to suppress centriole amplification. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262730 |
Ser83 |
VEQELPSsPKQPICF |
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27065328 |
Mechanistically, Cep76 phosphorylation inhibits activation of polo-like kinase 1 (Plk1), thereby blocking premature centriole disengagement and subsequent amplification. we conclude that Cep76 inhibits centriole disengagement and consequently amplification by blocking Plk1 activation at the centrosome. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CEP76 | down-regulates activity
binding
|
PLK1 |
0.408 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262731 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
27065329 |
Here, we found that centrosomal protein of 76 kDa (Cep76), previously shown to restrain centriole amplification, interacts with cyclin-dependent kinase 2 (CDK2) and is a bona fide substrate of this kinase. Cep76 is preferentially phosphorylated by cyclin A/CDK2 at a single site S83, and this event is crucial to suppress centriole amplification in S phase. Mechanistically, Cep76 phosphorylation inhibits activation of polo-like kinase 1 (Plk1), thereby blocking premature centriole disengagement and subsequent amplification. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |