Affordable Access

deepdyve-link
Publisher Website

PP2A Counterbalances Phosphorylation of pRB and Mitotic Proteins by Multiple CDKs: Potential Implications for PP2A Disruption in Cancer.

Authors
  • Kurimchak, Alison
  • Graña, Xavier
Type
Published Article
Journal
Genes & cancer
Publication Date
Nov 01, 2012
Volume
3
Issue
11-12
Pages
739–748
Identifiers
DOI: 10.1177/1947601912473479
PMID: 23634261
Source
Medline
Keywords
License
Unknown

Abstract

Protein Phosphatase 2A (PP2A) consists of a collection of heterotrimeric serine/threonine phosphatase holoenzymes that play multiple roles in cell signaling via dephosphorylation of numerous substrates of a large family of serine/threonine kinases. PP2A substrate specificity is mediated by B regulatory subunits of four different families, which selectively recognize diverse substrates by mechanisms that are not well understood. Among the many signaling pathways with critical PP2A functions are several deregulated in cancer cells, and PP2A is a know tumor suppressor. However, the precise composition of the heterotrimeric PP2A complexes with tumor supressor activity is not well understood. This review is centered on the emerging role of the B regulatory subunit B55α and related subfamilly members in the modulation of the phosphorylation state of pocket proteins and mitotic CDK substrates, as well as the implications of PP2A function disruption in cancer in the context of these activities.

Report this publication

Statistics

Seen <100 times