RT Journal Article
T1 Role of the Holoenzyme PP1-SPN in the Dephosphorylation of the RB Family of Tumor Suppressors During Cell Cycle.
A1 Verdugo-Sivianes, Eva M
A1 Carnero, Amancio
K1 PPP1R9B
K1 RB family proteins
K1 cancer
K1 cell cycle
K1 phosphatase PP1
K1 pocket proteins
K1 spinophilin
K1 tumorigenesis
AB Cell cycle progression is highly regulated by modulating the phosphorylation status of the retinoblastoma protein (pRB) and the other two members of the RB family, p107 and p130. This process is controlled by a balance in the action of kinases, such as the complexes formed by cyclin-dependent kinases (CDKs) and cyclins, and phosphatases, mainly the protein phosphatase 1 (PP1). However, while the phosphorylation of the RB family has been largely studied, its dephosphorylation is less known. Phosphatases are holoenzymes formed by a catalytic subunit and a regulatory protein with substrate specificity. Recently, the PP1-Spinophilin (SPN) holoenzyme has been described as the main phosphatase responsible for the dephosphorylation of RB proteins during the G0/G1 transition and at the end of G1. Moreover, SPN has been described as a tumor suppressor dependent on PP1 in lung and breast tumors, where it promotes tumorigenesis by increasing the cancer stem cell pool. Therefore, a connection between the cell cycle and stem cell biology has also been proposed via SPN/PP1/RB proteins.
SN 2072-6694
YR 2021
FD 2021-05-06
LK https://hdl.handle.net/10668/27893
UL https://hdl.handle.net/10668/27893
LA en
DS RISalud
RD Apr 19, 2025