Multiple paxillin binding sites regulate FAK function Public Deposited

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Creator
  • Schaller, Michael D.
    • Affiliation: N.C. Cancer Hospital, UNC Lineberger Comprehensive Cancer Center, School of Medicine, Department of Cell Biology and Physiology
  • Harrell, Jessica R
    • Affiliation: School of Medicine, Department of Cell Biology and Physiology
  • Gao, Guanghua
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
  • Rajfur, Zenon
    • Affiliation: School of Medicine, Department of Cell Biology and Physiology
  • Scheswohl, Danielle M
    • Affiliation: School of Medicine, Department of Cell Biology and Physiology
  • Campbell, Sharon
    • Affiliation: N.C. Cancer Hospital, UNC Lineberger Comprehensive Cancer Center, School of Medicine, Department of Biochemistry and Biophysics
Abstract
  • Abstract Background FAK localization to focal adhesions is essential for its activation and function. Localization of FAK is mediated through the C-terminal focal adhesion targeting (FAT) domain. Recent structural analyses have revealed two paxillin-binding sites in the FAT domain of FAK. To define the role of paxillin binding to each site on FAK, point mutations have been engineered to specifically disrupt paxillin binding to each docking site on the FAT domain of FAK individually or in combination. Results These mutants have been characterized and reveal an important role for paxillin binding in FAK subcellular localization and signaling. One paxillin-binding site (comprised of α-helices 1 and 4 of the FAT domain) plays a more prominent role in localization than the other. Mutation of either paxillin-binding site has similar effects on FAK activation and downstream signaling. However, the sites aren't strictly redundant as each mutant exhibits phosphorylation/signaling defects distinct from wild type FAK and a mutant completely defective for paxillin binding. Conclusion The studies demonstrate that the two paxillin-binding sites of FAK are not redundant and that both sites are required for FAK function.
Date of publication
Identifier
  • doi:10.1186/1750-2187-3-1
  • 18171471
Resource type
  • Article
Rights statement
  • In Copyright
Rights holder
  • Danielle M Scheswohl et al.; licensee BioMed Central Ltd.
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Journal title
  • Journal of Molecular Signaling
Journal volume
  • 3
Journal issue
  • 1
Page start
  • 1
Language
  • English
Is the article or chapter peer-reviewed?
  • Yes
ISSN
  • 1750-2187
Bibliographic citation
  • Journal of Molecular Signaling. 2008 Jan 02;3(1):1
Access
  • Open Access
Publisher
  • BioMed Central Ltd
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