Functional characterization of KIN-32, the Caenorhabditis elegans homolog of focal adhesion kinase.
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.
Cram
Erin J
EJ
Department of Biology, Northeastern University, Boston, Massachusetts 02115, USA. e.cram@neu.edu
Fontanez
Kristina Marie
KM
Schwarzbauer
Jean E
JE
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000201:enzymology* / Q000235:genetics; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry / Q000378:metabolism*; D045744:Cell Line, Tumor; D005347:Fibroblasts / Q000166:cytology / Q000201:enzymology; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism*; D022001:Focal Adhesions / Q000378:metabolism*; D017353:Gene Deletion; D015870:Gene Expression; D051379:Mice; D041681:NIH 3T3 Cells; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D016415:Sequence Alignment; D014162:Transfection
D029742:Caenorhabditis elegans Proteins; D051416:Focal Adhesion Protein-Tyrosine Kinases