Please use this identifier to cite or link to this item:
Title: Role of the Holoenzyme PP1-SPN in the Dephosphorylation of the RB Family of Tumor Suppressors During Cell Cycle.
Authors: Verdugo-Sivianes, Eva M
Carnero, Amancio
Keywords: PPP1R9B;RB family proteins;cancer;cell cycle;phosphatase PP1;pocket proteins;spinophilin;tumorigenesis
Issue Date: 6-May-2021
Abstract: 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.
metadata.dc.identifier.doi: 10.3390/cancers13092226
ISSN: 2072-6694
Appears in Collections:Producción 2020

Files in This Item:
File SizeFormat 
PMC8124259.pdf1,65 MBAdobe PDFView/Open

This item is protected by original copyright

This item is licensed under a Creative Commons License Creative Commons