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In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
Published on: June 28, 2019
The CHEVI tethering complex: facilitating special deliveries
Clare Rogerson1,2, Paul Gissen3,4,5
1MRC Laboratory for Molecular Cell Biology, University College London, London, UK.
Insights
The CHEVI complex, comprising VPS33B and VIPAR, plays a role in endosomal trafficking. New research shows it
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Interactions
Background:
- The class C Homologues in Endosome-Vesicle Interaction (CHEVI) complex, composed of VPS33B and VIPAR, is a recently identified tethering complex involved in endosomal trafficking.
- Its precise function, particularly in specialized cellular processes like megakaryocyte α-granule biogenesis, remains under investigation, distinct from known HOPS and CORVET complexes.
Purpose of the Study:
- To investigate the role of the CHEVI complex in α-granule biogenesis within megakaryocytes.
- To identify novel interactors of the CHEVI complex and elucidate their functional significance.
- To determine the requirement of VPS33B for the localization of specific proteins and cargo within megakaryocytes.
Main Methods:
- Immunofluorescence microscopy to visualize protein localization.
- Co-immunoprecipitation assays to identify protein interactions.
- Analysis of megakaryocyte proplatelets to assess cargo transport.
Main Results:
- The study identified α-tubulin and SEC22B as novel interactors of the CHEVI complex.
- VPS33B expression was found to be essential for the correct localization of SEC22B and von Willebrand factor (VWF) to proplatelets.
- These findings highlight the CHEVI complex's involvement in the specialized delivery of α-granule cargo.
Conclusions:
- The CHEVI complex, through VPS33B, plays a critical role in the biogenesis of α-granules in megakaryocytes.
- VPS33B mediates the localization of SEC22B and VWF, crucial for platelet formation.
- This research expands our understanding of the CHEVI complex's function in cargo trafficking across different cell types.
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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