Mutant FGFR3 associated with SADDAN disease causes cytoskeleton disorganization through PLCγ1/Src-mediated paxillin hyperphosphorylation-Reference-Cited by-同舟云学术

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Mutant FGFR3 associated with SADDAN disease causes cytoskeleton disorganization through PLCγ1/Src-mediated paxillin hyperphosphorylation

Published:2018-02 Issue: Volume:95 Page:17-26
ISSN:1357-2725
Container-title:The International Journal of Biochemistry & Cell Biology
language:en
Short-container-title:The International Journal of Biochemistry & Cell Biology

Author:

Montone R.,Romanelli M.G.,Baruzzi A.,Ferrarini F.,Liboi E.,Lievens P.M.-J.

Funder

Italian Association for Cancer Research

University of Verona Research Founding

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry

Reference67 articles.

1. Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase;Bellis;J. Biol. Chem.,1995

2. Severe achondroplasia with developmental delay and acanthosis nigricans (SADDAN): phenotypic analysis of a new skeletal dysplasia caused by a Lys650Met mutation in fibroblast growth factor receptor 3;Bellus;Am. J. Med. Genet.,1999

3. The localization of FGFR3 mutations causing thanatophoric dysplasia type I differentially affects phosphorylation, processing and ubiquitylation of the receptor;Bonaventure;FEBS J.,2007

4. Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin;Brown;Mol. Biol. Cell,1998

5. Focal adhesions, contractility, and signaling;Burridge;Annu. Rev. Cell Dev. Biol.,1996

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