C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol 2002 May 14;12(10):787-97
Date
05/17/2002Pubmed ID
12015115DOI
10.1016/s0960-9822(02)00810-2Scopus ID
2-s2.0-0037076211 (requires institutional sign-in at Scopus site) 258 CitationsAbstract
BACKGROUND: Mammalian integrin-linked kinase (ILK) was identified in a yeast two-hybrid screen for proteins binding the integrin beta(1) subunit cytoplasmic domain. ILK has been implicated in integrin-mediated signaling and is also an adaptor within integrin-associated cytoskeletal complexes.
RESULTS: We identified the C. elegans pat-4 gene in previous genetic screens for mutants unable to assemble integrin-mediated muscle cell attachments. Here, we report that pat-4 encodes the sole C. elegans homolog of ILK. In pat-4 null mutants, embryonic muscle cells form integrin foci, but the subsequent recruitment of vinculin and UNC-89 as well as actin and myosin filaments to these in vivo focal adhesion analogs is blocked. Conversely, PAT-4/ILK requires the ECM component UNC-52/perlecan, the transmembrane protein integrin, and the novel cytoplasmic attachment protein UNC-112 to be properly recruited to nascent attachments. Transgenically expressed "kinase-dead" ILK fully rescues pat-4 loss-of-function mutants. We also identify UNC-112 as a new binding partner for ILK.
CONCLUSIONS: Our data strengthens the emerging view that ILK functions primarily as an adaptor protein within integrin adhesion complexes and identifies UNC-112 as a new ILK binding partner.
Author List
Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BDMESH terms used to index this publication - Major topics in bold
AnimalsCaenorhabditis elegans
Caenorhabditis elegans Proteins
Carrier Proteins
Cell Adhesion
Cell Adhesion Molecules
Cytoskeleton
Focal Adhesions
Heparan Sulfate Proteoglycans
Integrins
Macromolecular Substances
Muscles
Mutation
Polymerase Chain Reaction
Protein Binding
Two-Hybrid System Techniques
Vinculin
