title: The CHEVI tethering complex: facilitating special deliveries.
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.
authors.affiliation: MRC Laboratory for Molecular Cell Biology, University College London, London, UK.|Institute of Child Health, University College London, London, UK.
authors.forename: Clare
authors.initials: C
authors.lastname: Rogerson
authors.affiliation: MRC Laboratory for Molecular Cell Biology, University College London, London, UK. p.gissen@ucl.ac.uk.|Institute of Child Health, University College London, London, UK. p.gissen@ucl.ac.uk.|Inherited Metabolic Diseases Unit, Great Ormond Street Hospital, London, UK. p.gissen@ucl.ac.uk.
authors.forename: Paul
authors.initials: P
authors.lastname: Gissen
mesh_terms: D000818:Animals; D006801:Humans; D008533:Megakaryocytes; D021381:Protein Transport; D006113:United Kingdom
keywords: CHEVI complex; VIPAR; VPS33B; megakaryocyte; platelet; tethering complexes; vesicle trafficking; α-granules