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Molecular insights into tether function at the late endosome and vacuole
Author(s) -
Ungermann Christian
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.463.3
Subject(s) - rab , endomembrane system , endosome , vacuole , microbiology and biotechnology , lipid bilayer fusion , small gtpase , tethering , gtpase , vesicle fusion , vesicle , vesicular transport proteins , chemistry , membrane , biology , biochemistry , synaptic vesicle , cytoplasm , signal transduction , intracellular , vacuolar protein sorting
Membrane fusion within the eukaryotic endomembrane system depends on the initial recognition of Rab GTPase on transport vesicles by multisubunit tethering complexes (MTC) and subsequent coupling to SNARE‐mediated fusion. The conserved vacuolar/lysosomal HOPS tethering complex combines both activities. Here, I will present insights into HOPS targeting to endosomal membranes, its regulation by phosphorylation, and its overall structure. Our data reveal that HOPS has a flexible elongated structure. I will show the localization of the individual subunits and the Rab binding site. Based on these findings, I will present a model how HOPS can tether membranes and support membrane fusion at late endosomes and vacuoles.