Details:

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.
Rogerson C., Gissen P., The Journal of Pathology.

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Our Involvement:

• Year: 2016
• Client: UCL - MRC Laboratory for Molecular Cell Biology - Prof.Paul Gissen
• Services: 2D illustration