The <scp>CHEVI</scp> tethering complex: facilitating special deliveries

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  • Clare Rogerson
    MRC Laboratory for Molecular Cell Biology University College London London UK
  • Paul Gissen
    MRC Laboratory for Molecular Cell Biology University College London London UK

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<jats:title>Abstract</jats:title><jats:p><jats:styled-content style="fixed-case">VPS33B</jats:styled-content> and <jats:styled-content style="fixed-case">VIPAR</jats:styled-content> comprise the two known components of the recently christened class C Homologues in Endosome–Vesicle Interaction (<jats:styled-content style="fixed-case">CHEVI</jats:styled-content>) complex, thought to act as a tethering complex in endosomal trafficking distinct from the <jats:styled-content style="fixed-case">HOPS</jats:styled-content> and <jats:styled-content style="fixed-case">CORVET</jats:styled-content> complexes in mammalian cells. A recent paper in <jats:italic>The Journal of Pathology</jats:italic> further explores the role of the <jats:styled-content style="fixed-case">CHEVI</jats:styled-content> complex in the biogenesis of α‐granules in megakaryocytes, identifying two novel interactors of this complex: α‐tubulin and SEC22B, and demonstrating that VPS33B expression is required for the localization of <jats:styled-content style="fixed-case">SEC22B</jats:styled-content> and the α‐granule cargo <jats:styled-content style="fixed-case">VWF</jats:styled-content> to proplatelets in megakaryocytes. These findings advance the current knowledge of the function of the <jats:styled-content style="fixed-case">CHEVI</jats:styled-content> complex in α‐granule biogenesis and together with studies in other systems, corroborate its role in the specialized delivery of cargo in different cell types. Copyright © 2016 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.</jats:p>

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