Protein Kinases and Phosphatases in the Control of Cell Fate

Protein Kinases and Phosphatases in the Control of Cell Fate

Protein phosphorylation controls many aspects of cell fate and is often deregulated in pathological conditions. Several recent findings have provided an intriguing insight into the spatial regulation of protein phosphorylation across different subcellular compartments and how this can be finely orch...

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Main Authors: Bononi, Angela, Agnoletto, Chiara, De Marchi, Elena, Marchi, Saverio, Patergnani, Simone, Bonora, Massimo, Giorgi, Carlotta, Missiroli, Sonia, Poletti, Federica, Rimessi, Alessandro, Pinton, Paolo
Format: Online
Language:English
Published: SAGE-Hindawi Access to Research 2011
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166778/
id pubmed-3166778
recordtype oai_dc
spelling pubmed-31667782011-09-08 Protein Kinases and Phosphatases in the Control of Cell Fate Bononi, Angela Agnoletto, Chiara De Marchi, Elena Marchi, Saverio Patergnani, Simone Bonora, Massimo Giorgi, Carlotta Missiroli, Sonia Poletti, Federica Rimessi, Alessandro Pinton, Paolo Review Article Protein phosphorylation controls many aspects of cell fate and is often deregulated in pathological conditions. Several recent findings have provided an intriguing insight into the spatial regulation of protein phosphorylation across different subcellular compartments and how this can be finely orchestrated by specific kinases and phosphatases. In this review, the focus will be placed on (i) the phosphoinositide 3-kinase (PI3K) pathway, specifically on the kinases Akt and mTOR and on the phosphatases PP2a and PTEN, and on (ii) the PKC family of serine/threonine kinases. We will look at general aspects of cell physiology controlled by these kinases and phosphatases, highlighting the signalling pathways that drive cell division, proliferation, and apoptosis. SAGE-Hindawi Access to Research 2011 2011-09-04 /pmc/articles/PMC3166778/ /pubmed/21904669 http://dx.doi.org/10.4061/2011/329098 Text en Copyright © 2011 Angela Bononi et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Bononi, Angela
Agnoletto, Chiara
De Marchi, Elena
Marchi, Saverio
Patergnani, Simone
Bonora, Massimo
Giorgi, Carlotta
Missiroli, Sonia
Poletti, Federica
Rimessi, Alessandro
Pinton, Paolo
spellingShingle Bononi, Angela
Agnoletto, Chiara
De Marchi, Elena
Marchi, Saverio
Patergnani, Simone
Bonora, Massimo
Giorgi, Carlotta
Missiroli, Sonia
Poletti, Federica
Rimessi, Alessandro
Pinton, Paolo
Protein Kinases and Phosphatases in the Control of Cell Fate
author_facet Bononi, Angela
Agnoletto, Chiara
De Marchi, Elena
Marchi, Saverio
Patergnani, Simone
Bonora, Massimo
Giorgi, Carlotta
Missiroli, Sonia
Poletti, Federica
Rimessi, Alessandro
Pinton, Paolo
author_sort Bononi, Angela
title Protein Kinases and Phosphatases in the Control of Cell Fate
title_short Protein Kinases and Phosphatases in the Control of Cell Fate
title_full Protein Kinases and Phosphatases in the Control of Cell Fate
title_fullStr Protein Kinases and Phosphatases in the Control of Cell Fate
title_full_unstemmed Protein Kinases and Phosphatases in the Control of Cell Fate
title_sort protein kinases and phosphatases in the control of cell fate
description Protein phosphorylation controls many aspects of cell fate and is often deregulated in pathological conditions. Several recent findings have provided an intriguing insight into the spatial regulation of protein phosphorylation across different subcellular compartments and how this can be finely orchestrated by specific kinases and phosphatases. In this review, the focus will be placed on (i) the phosphoinositide 3-kinase (PI3K) pathway, specifically on the kinases Akt and mTOR and on the phosphatases PP2a and PTEN, and on (ii) the PKC family of serine/threonine kinases. We will look at general aspects of cell physiology controlled by these kinases and phosphatases, highlighting the signalling pathways that drive cell division, proliferation, and apoptosis.
publisher SAGE-Hindawi Access to Research
publishDate 2011
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3166778/
_version_ 1611473645402587136

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