Protein Kinases and Phosphatases in the Control of Cell Fate
Open Access
- 4 September 2011
- journal article
- Published by Hindawi Limited in Enzyme Research
- Vol. 2011, 1-26
- https://doi.org/10.4061/2011/329098
Abstract
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.Keywords
This publication has 280 references indexed in Scilit:
- Nuclear PTEN Regulates the APC-CDH1 Tumor-Suppressive Complex in a Phosphatase-Independent MannerCell, 2011
- Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino AcidsCell, 2010
- The role of the Atg1/ULK1 complex in autophagy regulationCurrent Opinion in Cell Biology, 2010
- ER–Golgi network—A future target for anti-cancer therapyLeukemia Research, 2009
- Akt kinase reducing endoplasmic reticulum Ca2+ release protects cells from Ca2+-dependent apoptotic stimuliBiochemical and Biophysical Research Communications, 2008
- Tenets of PTEN Tumor SuppressionCell, 2008
- AKT/PKB Signaling: Navigating DownstreamCell, 2007
- Ubiquitination Regulates PTEN Nuclear Import and Tumor SuppressionCell, 2007
- NEDD4-1 Is a Proto-Oncogenic Ubiquitin Ligase for PTENCell, 2007
- Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistanceBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2006