Phosphorylation of Paxillin LD4 Destabilizes Helix Formation and Inhibits Binding to Focal Adhesion Kinase
Author:
Affiliation:
1. Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, and Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi702103n
Reference48 articles.
1. Focal adhesion kinase: the first ten years
2. The role of focal-adhesion kinase in cancer — a new therapeutic opportunity
3. Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK.
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1. The explorations of dynamic interactions of paxillin at the focal adhesions;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2022-10
2. Paxillin S273 Phosphorylation Regulates Adhesion Dynamics and Cell Migration through a Common Protein Complex with PAK1 and βPIX;Scientific Reports;2019-08-07
3. Focal adhesion kinase-dependent focal adhesion recruitment of SH2 domains directs SRC into focal adhesions to regulate cell adhesion and migration;Scientific Reports;2015-12-18
4. Phosphorylation and turnover of paxillin in focal contacts is controlled by force and defines the dynamic state of the adhesion site;Cytoskeleton;2015-02
5. How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine–aspartic acid (LD) motifs;Biochemical Journal;2014-05-29
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