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Article

Vps41 functions as a molecular ruler for HOPS tethering complex-mediated membrane fusion.

Journal of cell science - 15 Apr 2025

König Caroline, Shvarev Dmitry, Gao Jieqiong, Haar Eduard, Susan Nicole, Auffarth Kathrin, Langemeyer Lars, Moeller Arne, Ungermann Christian

Abstract excerpt

Fusion at the lysosome (or the yeast vacuole) requires the conserved hexameric HOPS tethering complex. In the yeast Saccharomyces cerevisiae, HOPS binds to the vacuolar Rab7-like GTPase Ypt7 via its subunits Vps41 and Vps39 and supports fusion by promoting SNARE assembly. In contrast to its sister complex CORVET, the Ypt7-interacting domain of Vps41 in the HOPS complex is connected to the core by a long, extended...

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Topics

Saccharomyces cerevisiae Proteins
Membrane Fusion
Saccharomyces cerevisiae
Vesicular Transport Proteins
Vacuoles

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

rab GTP-Binding Proteins

Lysosomes

Mutation

Autophagy

Protein Binding

Source

Identifiers

PMID: 40159992
DOI: 10.1242/jcs.263788

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Vps41 functions as a molecular ruler for HOPS tethering complex-mediated membrane fusion.PMID 40159992Read ↗

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New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion.Semantic proximity Read ↗

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