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2017 ; 28
(2
): 322-332
Nephropedia Template TP
Lürick A
; Gao J
; Kuhlee A
; Yavavli E
; Langemeyer L
; Perz A
; Raunser S
; Ungermann C
Mol Biol Cell
2017[Jan]; 28
(2
): 322-332
PMID27852901
show ga
Membrane fusion at endomembranes requires cross-talk between Rab GTPases and
tethers to drive SNARE-mediated lipid bilayer mixing. Several tethers have
multiple Rab-binding sites with largely untested function. Here we dissected the
lysosomal HOPS complex as a tethering complex with just two binding sites for the
Rab7-like Ypt7 protein to determine their relevance for fusion. Using tethering
and fusion assays combined with HOPS mutants, we show that HOPS-dependent fusion
requires both Rab-binding sites, with Vps39 being the stronger Ypt7 interactor
than Vps41. The intrinsic amphipathic lipid packaging sensor (ALPS) motif within
HOPS Vps41, a target of the vacuolar kinase Yck3, is dispensable for tethering
and fusion but can affect tethering if phosphorylated. In combination, our data
demonstrate that a multivalent tethering complex uses its two Rab bindings to
determine the place of SNARE assembly and thus fusion at endomembranes.
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