Phosphatases in cell–matrix adhesion and migration
- 1 September 2003
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 4 (9) , 700-711
- https://doi.org/10.1038/nrm1199
Abstract
Many proteins that have been implicated in cell-matrix adhesion and cell migration are phosphorylated, which regulates their folding, enzymatic activities and protein-protein interactions. Although modulation of cell motility by kinases is well known, increasing evidence confirms that phosphatases are essential at each stage of the migration process. Phosphatases can control the formation and maintenance of the actin cytoskeleton, regulate small GTPase molecular switches, and modulate the dynamics of matrix-adhesion interaction, actin contraction, rear release and migratory directionality.Keywords
This publication has 131 references indexed in Scilit:
- Hepatocyte Growth Factor Receptor Tyrosine Kinase Met Is a Substrate of the Receptor Protein-tyrosine Phosphatase DEP-1Journal of Biological Chemistry, 2003
- Protein phosphatase‐2A restricts migration of Lewis lung carcinoma cells by modulating the phosphorylation of focal adhesion proteinsInternational Journal of Cancer, 2002
- The origins of protein phosphorylationNature Cell Biology, 2002
- Tumor Suppressor PTEN Mediates Sensing of Chemoattractant GradientsCell, 2002
- Specific SHP-2 partitioning in raft domains triggers integrin-mediated signaling via Rho activationThe Journal of cell biology, 2002
- Cofilin Produces Newly Polymerized Actin Filaments that Are Preferred for Dendritic Nucleation by the Arp2/3 ComplexCurrent Biology, 2002
- c-Jun N-terminal kinase is involved in motility of endothelial cellExperimental & Molecular Medicine, 2001
- Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell SignalingMolecular Cell, 2001
- Initial sequencing and analysis of the human genomeNature, 2001
- Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient miceNature, 1995