Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/59250
Title: Phosphorylation of unique domains of Src family of kinases
Author: Amata, Irene
Maffei, Mariano, 1985- 
Pons Vallès, Miquel
Keywords: Fosforilació
Proteïnes
Bioquímica
Phosphorylation
Proteins
Biochemistry
Issue Date: 30-Jun-2014
Publisher: Frontiers Media
Abstract: Members of the Src family of kinases (SFKs) are non-receptor tyrosine kinases involved in numerous signal transduction pathways. The catalytic, SH3 and SH2 domains are attached to the membrane-anchoring SH4 domain through the intrinsically disordered"Unique" domains, which exhibit strong sequence divergence among SFK members. In the last decade, structural and biochemical studies have begun to uncover the crucial role of the Unique domain in the regulation of SFK activity. This mini-review discusses what is known about the phosphorylation events taking place on the SFK Unique domains, and their biological relevance. The modulation by phosphorylation of biologically relevant inter- and intra- molecular interactions of Src, as well as the existence of complex phosphorylation/dephosphorylation patterns observed for the Unique domain of Src, reinforces the important functional role of the Unique domain in the regulation mechanisms of the Src kinases and, in a wider context, of intrinsically disordered regions in cellular processes.
Note: Reproducció del document publicat a: http://dx.doi.org/10.3389/fgene.2014.00181
It is part of: Frontiers in Genetics, 2014, vol. 5, num. 181, p. 1-6
Related resource: http://dx.doi.org/10.3389/fgene.2014.00181
URI: http://hdl.handle.net/2445/59250
ISSN: 1664-8021
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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