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Are RB proteins a potential substrate of Pin1 in the regulation of the cell cycle?
Author(s) -
Gallo Gaia,
Giordano Antonio
Publication year - 2005
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.20451
Subject(s) - pin1 , phosphorylation , e2f , cyclin dependent kinase , microbiology and biotechnology , chemistry , cyclin a , cell cycle , biology , biochemistry , cell , isomerase , enzyme
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. © 2005 Wiley‐Liss, Inc.