Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 33, Pages 13345-13350Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1307074110
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Funding
- Royal Commission for the Exhibition
- Sir Henry Dale Fellowship
- Wellcome Trust [090909/Z/09/Z, 100140]
- Royal Society [098406/Z/12/Z]
- European Molecular Biology Organization
- Federation of the Society of Biochemistry Long-Term Fellowship
- Federation of the Society of Molecular Biology Long-Term Fellowship
- UK Medical Research Council Program Grant [G0900113]
- MRC [G0900113] Funding Source: UKRI
- Medical Research Council [G0900113] Funding Source: researchfish
- Wellcome Trust [090909/Z/09/Z] Funding Source: Wellcome Trust
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The multisubunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is required for late endosome-lysosome and autophagosome-lysosome fusion in mammals. We have determined the crystal structure of the human HOPS subunit Vps33A, confirming its identity as a Sec1/Munc18 family member. We show that HOPS subunit Vps16 recruits Vps33A to the human HOPS complex and that residues 642-736 are necessary and sufficient for this interaction, and we present the crystal structure of Vps33A in complex with Vps16(642-736). Mutations at the binding interface disrupt the Vps33A-Vps16 interaction both in vitro and in cells, preventing recruitment of Vps33A to the HOPS complex. The Vps33A-Vps16 complex provides a structural framework for studying the association between Sec1/Munc18 proteins and tethering complexes.
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