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Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion with Endosomes and Autophagosomes
Author(s) -
Wartosch Lena,
Günesdogan Ufuk,
Graham Stephen C.,
Luzio J. Paul
Publication year - 2015
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12283
Subject(s) - endosome , microbiology and biotechnology , lysosome , biology , lipid bilayer fusion , fusion protein , endocytic cycle , protein targeting , vacuole , intracellular , endocytosis , biochemistry , membrane protein , cell , cytoplasm , recombinant dna , enzyme , membrane , gene
In yeast the homotypic fusion and vacuole protein sorting ( HOPS ) complex is a tether required for vacuole fusion. We show that all proteins of the mammalian HOPS complex are necessary for fusion of lysosomes with endosomes and that recruitment of the Sec1/Munc18 ( SM ) protein VPS33A to the complex via VPS16 is essential for this and for fusion of lysosomes with autophagosomes. Mammalian VPS33B and VIPAR are not required for these fusion events and are not part of the HOPS or the class C core vacuole/endosome tethering ( CORVET ) complexes, but form a separate complex.