The Sec1/Munc18 Protein Groove Plays a Conserved Role in Interaction with Sec9p/ SNAP ‐25 | Zendy

WeberBoyvat Marion | Zendy; Chernov Konstantin G. | Zendy; Aro Nina | Zendy; Wohlfahrt Gerd | Zendy; Olkkonen Vesa M. | Zendy; Jäntti Jussi | Zendy

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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.

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