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• W2022131173 startingPage "2011" @default.
• W2022131173 abstract "ADAM (a disintegrin and metalloprotease) family proteins play important roles in animal development and pathogenesis [1Seals D.F. Courtneidge S.A. The ADAMs family of metalloproteases Multidomain proteins with multiple functions.Genes Dev. 2003; 17: 7-30Crossref PubMed Scopus (843) Google Scholar]. In C. elegans, a secreted ADAM protein, MIG-17, acts from outside the gonad to control the migration of gonadal distal tip cells (DTCs) that promote gonad morphogenesis [2Nishiwaki K. Hisamoto N. Matsumoto K. A metalloprotease disintegrin that controls cell migration in Caenorhabditis elegans.Science. 2000; 288: 2205-2208Crossref PubMed Scopus (93) Google Scholar]. Here, we report that dominant mutations in the fbl-1 gene encoding fibulin-1 spliced isoforms, which are calcium binding extracellular matrix proteins, bypass the requirement for MIG-17 activity in directing DTC migration. Specific amino acid substitutions in the third EGF-like motif of one of the two isoforms, FBL-1C, which corresponds to mammalian fibulin-1C, suppress mig-17 mutations. FBL-1C is synthesized in the gut cells and localizes strongly to the gonadal basement membrane in a MIG-17-dependent manner. Localization of mutant FBL-1C is weaker than that of the wild-type protein and is insensitive to MIG-17 activity, suggesting that it gains a novel function that compensates for its reduced molecular density. We propose that proteolysis by MIG-17 recruits FBL-1C to the gonadal basement membrane, where it is required for the guidance of DTCs, and that mutant FBL-1C acts in a manner that mimics the downstream events of MIG-17-mediated proteolysis." @default.
• W2022131173 created "2016-06-24" @default.
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• W2022131173 date "2004-11-01" @default.
• W2022131173 modified "2023-09-23" @default.
• W2022131173 title "A Fibulin-1 Homolog Interacts with an ADAM Protease that Controls Cell Migration in C. elegans" @default.
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• W2022131173 doi "https://doi.org/10.1016/j.cub.2004.10.047" @default.
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