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, G., & Giordano, A. (2005). Are RB proteins a potential substrate of Pin1 in the regulation of the cell cycle?. JOURNAL OF CELLULAR PHYSIOLOGY, 205(2), 176-181.

Are RB proteins a potential substrate of Pin1 in the regulation of the cell cycle?

GIORDANO, ANTONIO
2005

Abstract

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.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/11378
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo