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C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes.
Curr Biol. 2002 May 14; 12(10):787-97.CB

Abstract

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.

Authors+Show Affiliations

Department of Cell and Structural Biology, University of Illinois, Urbana-Champaign, 601 South Goodwin Avenue, Urbana, IL 61801, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

12015115

Citation

Mackinnon, A Craig, et al. "C. Elegans PAT-4/ILK Functions as an Adaptor Protein Within Integrin Adhesion Complexes." Current Biology : CB, vol. 12, no. 10, 2002, pp. 787-97.
Mackinnon AC, Qadota H, Norman KR, et al. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol. 2002;12(10):787-97.
Mackinnon, A. C., Qadota, H., Norman, K. R., Moerman, D. G., & Williams, B. D. (2002). C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Current Biology : CB, 12(10), 787-97.
Mackinnon AC, et al. C. Elegans PAT-4/ILK Functions as an Adaptor Protein Within Integrin Adhesion Complexes. Curr Biol. 2002 May 14;12(10):787-97. PubMed PMID: 12015115.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. AU - Mackinnon,A Craig, AU - Qadota,Hiroshi, AU - Norman,Kenneth R, AU - Moerman,Donald G, AU - Williams,Benjamin D, PY - 2002/5/17/pubmed PY - 2002/10/18/medline PY - 2002/5/17/entrez SP - 787 EP - 97 JF - Current biology : CB JO - Curr Biol VL - 12 IS - 10 N2 - 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. SN - 0960-9822 UR - https://www.unboundmedicine.com/medline/citation/12015115/C__elegans_PAT_4/ILK_functions_as_an_adaptor_protein_within_integrin_adhesion_complexes_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0960-9822(02)00810-2 DB - PRIME DP - Unbound Medicine ER -