Functional characterization of KIN-32, the Caenorhabditis elegans homolog of focal adhesion kinase

Erin J. Cram, Kristina Marie Fontanez, Jean E. Schwarzbauer

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

We have identified the single Caenorhabditis elegans focal adhesion kinase (FAK) homolog KIN-32, which has the signature FAK structure including an N-terminal Four.1-Ezrin-Radixin-Moesin (FERM) domain followed by a tyrosine kinase domain and a C-terminal domain with weak homology to the focal adhesion targeting domain. The functional requirements for KIN-32 were examined using RNA interference depletion experiments and analysis of a deletion allele, kin-32(ok166), in which a large segment of the FERM domain is missing. Our results show that reduced levels of expression or absence of the FERM domain do not affect viability, fertility, or anatomy in C. elegans. Expression of an analogous FERM deletion in mouse FAK showed kinase activity in vitro and supported normal focal adhesion localization in cell culture. Thus, the FERM domain of KIN-32, and possibly KIN-32 activity in general, appears to be dispensable for normal C. elegans physiology.

Original languageEnglish (US)
Pages (from-to)837-846
Number of pages10
JournalDevelopmental Dynamics
Volume237
Issue number3
DOIs
StatePublished - Mar 2008

All Science Journal Classification (ASJC) codes

  • Developmental Biology

Keywords

  • FAK
  • FERM
  • Kinase
  • Nematode
  • RNAi

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