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TitleStructure of the HOPS tethering complex, a lysosomal membrane fusion machinery.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateSep 13, 2022
AuthorsDmitry Shvarev / Jannis Schoppe / Caroline König / Angela Perz / Nadia Füllbrunn / Stephan Kiontke / Lars Langemeyer / Dovile Januliene / Kilian Schnelle / Daniel Kümmel / Florian Fröhlich / Arne Moeller / Christian Ungermann /
PubMed AbstractLysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a ...Lysosomes are essential for cellular recycling, nutrient signaling, autophagy, and pathogenic bacteria and viruses invasion. Lysosomal fusion is fundamental to cell survival and requires HOPS, a conserved heterohexameric tethering complex. On the membranes to be fused, HOPS binds small membrane-associated GTPases and assembles SNAREs for fusion, but how the complex fulfills its function remained speculative. Here, we used cryo-electron microscopy to reveal the structure of HOPS. Unlike previously reported, significant flexibility of HOPS is confined to its extremities, where GTPase binding occurs. The SNARE-binding module is firmly attached to the core, therefore, ideally positioned between the membranes to catalyze fusion. Our data suggest a model for how HOPS fulfills its dual functionality of tethering and fusion and indicate why it is an essential part of the membrane fusion machinery.
External linksElife / PubMed:36098503 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.89 - 5.0 Å
Structure data

EMDB-14965: HOPS tethering complex from yeast, consensus map covering the upper part of the complex
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-14966: HOPS tethering complex from yeast, consensus map covering the bottom part of the complex
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-14967: HOPS tethering complex from yeast, local refinement map of the SNARE-binding module
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-14968: HOPS tethering complex from yeast, local refinement map of the backbone part of the complex
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-14969: HOPS tethering complex from yeast, local refinement map of the bottom part of the complex (Vps18)
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-14970: HOPS tethering complex from yeast, local refinement map of the bottom part of the complex (Vps39)
Method: EM (single particle) / Resolution: 5.0 Å

PDB-7zty:
Structure of Vps39 N-terminal domain from Chaetomium thermophilum
Method: X-RAY DIFFRACTION / Resolution: 2.89 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • chaetomium thermophilum (fungus)
KeywordsTRANSPORT PROTEIN / tethering / membrane fusion / GTPase effector / HOPS

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