The CHEVI tethering complex: facilitating special deliveries |
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| Authors: | Clare Rogerson Paul Gissen |
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| Affiliation: | 1. MRC Laboratory for Molecular Cell Biology, University College London, London, UK;2. Institute of Child Health, University College London, London, UK;3. Inherited Metabolic Diseases Unit, Great Ormond Street Hospital, London, UK |
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| Abstract: | VPS33B and VIPAR comprise the two known components of the recently christened class C Homologues in Endosome–Vesicle Interaction (CHEVI) complex, thought to act as a tethering complex in endosomal trafficking distinct from the HOPS and CORVET complexes in mammalian cells. A recent paper in The Journal of Pathology further explores the role of the CHEVI 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 SEC22B and the α‐granule cargo VWF to proplatelets in megakaryocytes. These findings advance the current knowledge of the function of the CHEVI 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. |
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| Keywords: | VPS33B VIPAR vesicle trafficking tethering complexes megakaryocyte platelet α ‐granules CHEVI complex |
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