Closing in on the biological functions of fps/fes and fer
- 1 April 2002
- journal article
- review article
- Published by Springer Nature in Nature Reviews Molecular Cell Biology
- Vol. 3 (4) , 278-289
- https://doi.org/10.1038/nrm783
Abstract
Fps/Fes and Fer are the only known members of a distinct subfamily of the non-receptor protein-tyrosine kinase family. Recent studies indicate that these kinases have roles in regulating cytoskeletal rearrangements and inside out signalling that accompany receptor ligand, cell matrix and cell cell interactions. Genetic analysis using transgenic mouse models also implicates these kinases in the regulation of inflammation and innate immunity.Keywords
This publication has 96 references indexed in Scilit:
- Attenuation of Adhesion-dependent Signaling and Cell Spreading in Transformed Fibroblasts Lacking Protein Tyrosine Phosphatase-1BJournal of Biological Chemistry, 2001
- Subcellular Localization Analysis of the Closely Related Fps/Fes and Fer Protein-Tyrosine Kinases Suggests a Distinct Role for Fps/Fes in Vesicular TraffickingExperimental Cell Research, 2001
- The Nonreceptor Protein-tyrosine Kinase c-Fes Is Involved in Fibroblast Growth Factor-2-induced Chemotaxis of Murine Brain Capillary Endothelial CellsJournal of Biological Chemistry, 2000
- Three-dimensional structure of the tyrosine kinase c-SrcNature, 1997
- Co-expression with BCR Induces Activation of the FES Tyrosine Kinase and Phosphorylation of Specific N-terminal BCR Tyrosine ResiduesPublished by Elsevier ,1996
- Autophosphorylation of the Fes Tyrosine KinasePublished by Elsevier ,1996
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanismBiochemistry, 1993
- Nucleotide sequence and topography of chicken c-fpsJournal of Molecular Biology, 1985
- Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesisCell, 1984