The conserved oligomeric Golgi complex acts in organ morphogenesis via glycosylation of an ADAM protease in C. elegans

Yukihiko Kubota, Mitsue Sano, Saori Goda, Norio Suzuki, Kiyoji Nishiwaki

    Research output: Contribution to journalArticle

    46 Citations (Scopus)

    Abstract

    In C. elegans, the gonad acquires two U-shaped arms through directed migration of gonadal distal tip cells (DTCs). A member of the ADAM (a disintegrin and metalloprotease) family, MIG-17, is secreted from muscle cells and localizes to the gonadal basement membrane where it functions in DTC migration. Mutations in cogc-3 and cogc-1 cause misdirected DTC migration similar to that seen in mig-17 mutants. Here, we report that COGC-3 and COGC-1 proteins are homologous to mammalian COG-3/Sec34 and COG-1/IdIBp, respectively, two of the eight components of the conserved oligomeric Golgi (COG) complex required for Golgi function. Knockdown of any of the other six components by RNA interference also produces DTC migration defects, suggesting that the eight components function in a common pathway. COGC-3 and COGC-1 are required for the glycosylation and gonadal localization of MIG-17, but not for secretion of MIG-17 from muscle cells. Furthermore, COGC-3 requires MIG-17 activity for its action in DTC migration. Our findings demonstrate that COG complex-dependent glycosylation of an ADAM protease plays a crucial role in determining organ shape.

    Original languageEnglish
    Pages (from-to)263-273
    Number of pages11
    JournalDevelopment
    Volume133
    Issue number2
    DOIs
    Publication statusPublished - 2006 Jan 1

    Keywords

    • ADAM protease
    • C. elegans
    • COG complex
    • Glycosylation
    • Organogenesis

    ASJC Scopus subject areas

    • Molecular Biology
    • Developmental Biology

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