Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
