Regulation of PP2A by Sphingolipid Metabolism and Signaling

Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase that is a primary regulator of cellular proliferation through targeting of proliferative kinases, cell cycle regulators, and apoptosis inhibitors. It is through the regulation of these regulatory elements that gives PP2A tumor suppresso...

Full description

Bibliographic Details
Main Authors: Joshua eOaks, Besim eOgretmen
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-01-01
Series:Frontiers in Oncology
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fonc.2014.00388/full
_version_ 1819147940782931968
author Joshua eOaks
Besim eOgretmen
author_facet Joshua eOaks
Besim eOgretmen
author_sort Joshua eOaks
collection DOAJ
description Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase that is a primary regulator of cellular proliferation through targeting of proliferative kinases, cell cycle regulators, and apoptosis inhibitors. It is through the regulation of these regulatory elements that gives PP2A tumor suppressor functions. In addition to mutations on the regulatory subunits, the phosphatase/tumor suppressing activity of PP2A is also inhibited in several cancer types due to overexpression or modification of the endogenous PP2A inhibitors such as SET/I2PP2A. This review focuses on the current literature regarding the interactions between the lipid signaling molecules, selectively sphingolipids, and the PP2A inhibitor SET for the regulation of PP2A, and the therapeutic potential of sphingolipids as PP2A activators for tumor suppression via targeting SET oncoprotein.
first_indexed 2024-12-22T13:37:48Z
format Article
id doaj.art-e8c217fd32574405a79f68316bdf4c65
institution Directory Open Access Journal
issn 2234-943X
language English
last_indexed 2024-12-22T13:37:48Z
publishDate 2015-01-01
publisher Frontiers Media S.A.
record_format Article
series Frontiers in Oncology
spelling doaj.art-e8c217fd32574405a79f68316bdf4c652022-12-21T18:24:00ZengFrontiers Media S.A.Frontiers in Oncology2234-943X2015-01-01410.3389/fonc.2014.00388127225Regulation of PP2A by Sphingolipid Metabolism and SignalingJoshua eOaks0Besim eOgretmen1Medical University of South CarolinaMedical University of South CarolinaProtein phosphatase 2A (PP2A) is a serine/threonine phosphatase that is a primary regulator of cellular proliferation through targeting of proliferative kinases, cell cycle regulators, and apoptosis inhibitors. It is through the regulation of these regulatory elements that gives PP2A tumor suppressor functions. In addition to mutations on the regulatory subunits, the phosphatase/tumor suppressing activity of PP2A is also inhibited in several cancer types due to overexpression or modification of the endogenous PP2A inhibitors such as SET/I2PP2A. This review focuses on the current literature regarding the interactions between the lipid signaling molecules, selectively sphingolipids, and the PP2A inhibitor SET for the regulation of PP2A, and the therapeutic potential of sphingolipids as PP2A activators for tumor suppression via targeting SET oncoprotein.http://journal.frontiersin.org/Journal/10.3389/fonc.2014.00388/fullSphingolipidsceramidePP2AFTY720tumor suppression.
spellingShingle Joshua eOaks
Besim eOgretmen
Regulation of PP2A by Sphingolipid Metabolism and Signaling
Frontiers in Oncology
Sphingolipids
ceramide
PP2A
FTY720
tumor suppression.
title Regulation of PP2A by Sphingolipid Metabolism and Signaling
title_full Regulation of PP2A by Sphingolipid Metabolism and Signaling
title_fullStr Regulation of PP2A by Sphingolipid Metabolism and Signaling
title_full_unstemmed Regulation of PP2A by Sphingolipid Metabolism and Signaling
title_short Regulation of PP2A by Sphingolipid Metabolism and Signaling
title_sort regulation of pp2a by sphingolipid metabolism and signaling
topic Sphingolipids
ceramide
PP2A
FTY720
tumor suppression.
url http://journal.frontiersin.org/Journal/10.3389/fonc.2014.00388/full
work_keys_str_mv AT joshuaeoaks regulationofpp2abysphingolipidmetabolismandsignaling
AT besimeogretmen regulationofpp2abysphingolipidmetabolismandsignaling