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Author Notes:

Correspondence to: Victor Faundez; Email: vfaunde@emory.edu

Subject:

Research Funding:

This work was supported by grants from the National Institutes of Health to V.F. (NS42599 and GM077569) and S.W.L. (GM082932). S.A.Z. was supported by T32 GM008367, National Institutes of Health, Training Program in Biochemistry, Cell, and Molecular Biology.

Keywords:

  • HOPS
  • SPE-39
  • VIPAR
  • arthrogryposis
  • Hermansky-Pudlak
  • Vps33
  • Vps16B

Metazoan cell biology of the HOPS tethering complex

Tools:

Journal Title:

Cellular Logistics

Volume:

Volume 1, Number 3

Publisher:

, Pages 111-117

Type of Work:

Article | Post-print: After Peer Review

Abstract:

Membrane fusion with vacuoles, the lysosome equivalent of the yeast Saccharomyces cerevisiae, is among the best understood membrane fusion events. Our precise understanding of this fusion machinery stems from powerful genetics and elegant in vitro reconstitution assays. Central to vacuolar membrane fusion is the multi-subunit tether the HO motypic fusion and Protein Sorting (HOPS) complex, a complex of proteins that organizes other necessary components of the fusion machinery. We lack a similarly detailed molecular understanding of membrane fusion with lysosomes or lysosome-related organelles in metazoans. However, it is likely that fundamental principles of how rabs, SNAREs and HOPS tethers work to fuse membranes with lysosomes and related organelles are conserved between Saccharomyces cerevisiae and metazoans. Here, we discuss emerging differences in the coat-dependent mechanisms that govern HOPS complex subcellular distribution between Saccharomyces cerevisiae and metazoans. These differences reside upstream of the membrane fusion event. We propose that the differences in how coats segregate class C Vps/HOPS tethers to organelles and domains of metazoan cells are adaptations to complex architectures that characterize metazoan cells such as those of neuronal and epithelial tissues.

Copyright information:

© 2011 Landes Bioscience

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