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CAP

  • SHORT REPORT
    F-BAR domain protein Syndapin regulates actomyosin dynamics during apical cap remodeling in syncytial Drosophila embryos
    Aparna Sherlekar, Gayatri Mundhe, Prachi Richa, Bipasha Dey, Swati Sharma, Richa Rikhy
    Journal of Cell Science 2020 133: jcs235846 doi: 10.1242/jcs.235846 Published 26 May 2020

    Summary: Syndapin, an F-BAR domain protein, regulates the transition from Arp2/3-dependent protrusion remodeling and cap expansion to actomyosin-dependent cap buckling in the Drosophila blastoderm embryo.

  • RESEARCH ARTICLE
    Vinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation
    Takafumi Ichikawa, Masahiro Kita, Tsubasa S. Matsui, Ayaka Ichikawa Nagasato, Tomohiko Araki, Shian-Huey Chiang, Takuhito Sezaki, Yasuhisa Kimura, Kazumitsu Ueda, Shinji Deguchi, Alan R. Saltiel, Noriyuki Kioka
    Journal of Cell Science 2017 130: 3517-3531; doi: 10.1242/jcs.200691

    Summary: Comparing the functions of vinexin family (SORBS) proteins reveals that vinexin-α and CAP regulate vinculin behavior depending on the stiffness of the extracellular matrix, while ArgBP2 plays a role in generating greater contractile forces.

  • RESEARCH ARTICLE
    Srv2/CAP is required for polarized actin cable assembly and patch internalization during clathrin-mediated endocytosis
    Junko Y. Toshima, Chika Horikomi, Asuka Okada, Makiko N. Hatori, Makoto Nagano, Atsushi Masuda, Wataru Yamamoto, Daria Elisabeth Siekhaus, Jiro Toshima
    Journal of Cell Science 2016 129: 367-379; doi: 10.1242/jcs.176651

    Summary: Srv2/CAP is required for efficient endocytosis owing to its role in the formation of the actin patches that aid in vesicle invagination and in the formation of the actin cables that these move along.

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