The CHEVI tethering complex: facilitating special deliveries
0301 basic medicine
-granules
Hops
Mammalian Corvet
03 medical and health sciences
Vesicle Trafficking
Megakaryocyte
Maturation
Pathology
Tethering Complexes
Animals
Humans
Chevi Complex
Fusion
Vipar
Arthrogryposis
0303 health sciences
Science & Technology
Trafficking
Vps33b
Platelet
Renal Dysfunction
United Kingdom
Protein Transport
Oncology
Recruitment
Life Sciences & Biomedicine
Megakaryocytes
DOI:
10.1002/path.4785
Publication Date:
2016-08-24T08:26:50Z
AUTHORS (2)
ABSTRACT
AbstractVPS33B 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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