ArticleCellular logistics2014
Tracking of the dynamic localization of the Rab-specific HOPS subunits reveal their distinct interaction with Ypt7 and vacuoles.
Article in Cellular logistics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Loss of the putative Rab GTPase, Ypt7, impairs the virulence ofFrontiers in microbiology · 2024Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.Molecular biology of the cell · 2023Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.bioRxiv : the preprint server for biology · 2023Article
- Article
- Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021Article
- AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.The EMBO journal · 2020Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- The NaMolecular biology of the cell · 2018Article
- Multivalent Rab interactions determine tether-mediated membrane fusion.Molecular biology of the cell · 2017Article
- A HOPS Protein, MoVps41, Is Crucially Important for Vacuolar Morphogenesis, Vegetative Growth, Reproduction and Virulence inFrontiers in plant science · 2017Article
- Identification of a Rab GTPase-activating protein cascade that controls recycling of the Rab5 GTPase Vps21 from the vacuole.Molecular biology of the cell · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endosomal and vacuole fusion depends on the two homologous tethering complexes CORVET and HOPS. HOPS binds the activated Rab GTPase Ypt7 via two distinct subunits, Vps39 and Vps41. To understand the participation and possible polarity of Vps41 and Vps39 during tethering, we used an in vivo approach. For this, we established the ligand-induced relocalization to the plasma membrane, using the Mon1-Ccz1 GEF complex that activates Ypt7 on endosomes. We then employed slight overexpression to compare the mobility of the HOPS-specific Vps41 and Vps39 subunits during this process. Our data indicate an asymmetry in the Rab-specific interaction of the two HOPS subunits: Vps39 is more tightly bound to the vacuole, and relocalizes the entire vacuole to the plasma membrane, whereas Vps41 behaved like the more mobile subunit. This is due to their specific Rab binding, as the mobility of both subunits was similar in
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