The CHEVI tethering complex: facilitating special deliveries

J Pathol. 2016 Nov;240(3):249-252. doi: 10.1002/path.4785.

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.

Keywords: CHEVI complex; VIPAR; VPS33B; megakaryocyte; platelet; tethering complexes; vesicle trafficking; α-granules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Megakaryocytes*
  • Protein Transport*
  • United Kingdom