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• W2144859098 abstract "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.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.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." @default.
• W2144859098 created "2016-06-24" @default.
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• W2144859098 date "2002-05-01" @default.
• W2144859098 modified "2023-10-12" @default.
• W2144859098 title "C. elegans PAT-4/ILK Functions as an Adaptor Protein within Integrin Adhesion Complexes" @default.
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• W2144859098 doi "https://doi.org/10.1016/s0960-9822(02)00810-2" @default.
• W2144859098 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12015115" @default.
• W2144859098 hasPublicationYear "2002" @default.
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