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The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/ SNAP ‐25
Author(s) -
WeberBoyvat Marion,
Chernov Konstantin G.,
Aro Nina,
Wohlfahrt Gerd,
Olkkonen Vesa M.,
Jäntti Jussi
Publication year - 2016
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.12349
Subject(s) - biology , mutant , microbiology and biotechnology , vesicular transport proteins , lipid bilayer fusion , groove (engineering) , biophysics , saccharomyces cerevisiae , yeast , membrane , genetics , gene , materials science , vacuolar protein sorting , metallurgy
The events orchestrating vesicle targeting and fusion at the plasma membrane are poorly understood. The Sec1/Munc18 proteins have an essential role in SNARE ‐mediated membrane fusion. We show in yeast and mammalian cells that ‘the groove’, a recently identified protein interaction site in Sec1p, plays an important role in mediating interactions with Sec9p/ SNAP ‐25. ‘The groove’ represents an evolutionarily conserved site for Sec9p/ SNAP ‐25 binding and plays, in concert with Sro7p, a regulatory role in initial steps of exocytic SNARE complex assembly.