Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats

Tuula Klaavuniemi, Sawako Yamashiro, Shoichiro Ono

    Research output: Contribution to journalArticle

    17 Citations (Scopus)

    Abstract

    The gelsolin family of proteins is a major class of actin regulatory proteins that sever, cap, and nucleate actin filaments in a calcium-dependent manner and are involved in various cellular processes. Typically, gelsolin-related proteins have three or six repeats of gelsolin-like (G) domain, and each domain plays a distinct role in severing, capping, and nucleation. The Caenorhabditis elegans gelsolin-like protein-1 (gsnl-1) gene encodes an unconventional gelsolin-related protein with four G domains. Sequence alignment suggests that GSNL-1 lacks two G domains that are equivalent to fourth and fifth G domains of gelsolin. In vitro, GSNL-1 severed actin filaments and capped the barbed end in a calcium-dependent manner. However, unlike gelsolin, GSNL-1 remained bound to the side of F-actin with a submicromolar affinity and did not nucleate actin polymerization, although it bound to G-actin with high affinity. These results indicate that GSNL-1 is a novel member of the gelsolin family of actin regulatory proteins and provide new insight into functional diversity and evolution of gelsolin-related proteins.

    Original languageEnglish
    Pages (from-to)26071-26080
    Number of pages10
    JournalJournal of Biological Chemistry
    Volume283
    Issue number38
    DOIs
    Publication statusPublished - 2008 Sep 19

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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