Are RB proteins a potential substrate of Pin1 in the regulation of the cell cycle?
RB family members are post-transductionally regulated proteins and phosphorylation at Ser/Thr residues leads to their gradual inactivation. Cyclin/cdk complexes are mainly responsible for the regulation of these pocket proteins, which is crucial for release of E2F factor. Despite the fact that E2F release is a phosphorylation-dependent process, it is still not evident how phosphorylation physically determines the shift from the active to the inactive feature of RB molecules. We would like to put forward the hypothesis that Pin1 is involved in RB proteins phosphorylation and E2F release, suggesting an additional post-translational level of control on this family of molecules.
Gallo
Gaia
G
Department of Human Pathology and Oncology, University of Siena, Siena, Italy. gaiagallo@hotmail.com
Giordano
Antonio
A
D000818:Animals; D002453:Cell Cycle / Q000502:physiology*; D005544:Forecasting; D005786:Gene Expression Regulation; D006801:Humans; D008954:Models, Biological; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000378:metabolism*; D016160:Retinoblastoma Protein / Q000378:metabolism*; D013379:Substrate Specificity
D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D016160:Retinoblastoma Protein; C000606846:PIN1 protein, human; D019696:Peptidylprolyl Isomerase