Multiple Roles of VARP in Endosomal Trafficking: Rabs, Retromer Components and R-SNARE VAMP7 Meet on VARP

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    15 Citations (Scopus)

    Abstract

    VARP (VPS9-ankyrin-repeat protein, also known as ANKRD27) was originally identified as an N-terminal VPS9 (vacuolar protein sorting 9)-domain-containing protein that possesses guanine nucleotide exchange factor (GEF) activity toward small GTPase Rab21 and contains two ankyrin repeat (ANKR) domains in its central region. A number of VARP-interacting molecules have been identified during the past five years, and considerable attention is now being directed to the multiple roles of VARP in endosomal trafficking. More specifically, VARP is now known to interact with three different types of key membrane trafficking regulators, i.e. small GTPase Rabs (Rab32, Rab38 and Rab40C), the retromer complex (a sorting nexin dimer, VPS26, VPS29 and VPS35) and R-SNARE VAMP7. By binding to several of these molecules, VARP regulates endosomal trafficking, which underlies a variety of cellular events, including melanogenic enzyme trafficking to melanosomes, dendrite outgrowth of melanocytes, neurite outgrowth and retromer-mediated endosome-to-plasma membrane sorting of transmembrane proteins.

    Original languageEnglish
    Pages (from-to)709-719
    Number of pages11
    JournalTraffic
    Volume17
    Issue number7
    DOIs
    Publication statusPublished - 2016 Jul 1

    Keywords

    • Rab effector
    • SNARE
    • VPS9 domain
    • endosome
    • guanine nucleotide exchange factor
    • melanosome
    • membrane traffic
    • retromer
    • small GTPase Rab

    ASJC Scopus subject areas

    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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