We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The CHEVI tethering complex: facilitating special deliveries.
- Authors
Rogerson, Clare; Gissen, Paul
- 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.
- Publication
Journal of Pathology, 2016, Vol 240, Issue 3, p249
- ISSN
0022-3417
- Publication type
Article
- DOI
10.1002/path.4785