The Sec1/Munc18 protein groove plays a conserved role in interaction with Sec9p/SNAP-25

Marion Weber-Boyvat (Corresponding Author), Konstantin G. Chernov, Nina Aro, Gerd Wohlfahrt, Vesa M. Okkkonen, Jussi Jäntti (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

6 Citations (Scopus)

Abstract

The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNAREmediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here we show that a sec1 groove mutant yeast strain, sec1(w24), displays temperature sensitive growth and secretion defects. The yeast Sec1p and mammalian Munc18-1 grooves were shown to play an important role in the interaction with the SNAREs Sec9p and SNAP-25b, respectively. Incubation of SNAP-25b with Munc18-1 groove mutant resulted in a lag in the kinetics of SNARE complex assembly in vitro as compared to wild-type Munc18-1. The SNARE regulator SRO7 was identified as a multicopy suppressor of sec1(w24) groove mutant and an intact Sec1p groove was required for the plasma membrane targeting of Sro7p-SNARE complexes. Simultaneous inactivation of Sec1p groove and SRO7 resulted in reduced levels of exocytic SNARE complexes. Our results identify the groove as a conserved interaction surface in SM proteins. The results indicate that this structural element is important for interactions with Sec9p/SNAP-25 and participates, in concert with Sro7p, in the initial steps of SNARE complex assembly.
Original languageEnglish
Pages (from-to)131-153
JournalTraffic
Volume17
Issue number2
DOIs
Publication statusPublished - 2016
MoE publication typeA1 Journal article-refereed

Fingerprint

Munc18 Proteins
SNARE Proteins
Yeast
Yeasts
Membrane Fusion
Cell membranes
Proteins
Fusion reactions
Cell Membrane
Membranes
Defects
Kinetics
Temperature
Growth

Keywords

  • exocytosis
  • Sec1
  • Munc18
  • Sec9
  • SNAP-25
  • Sro7
  • Tomosyn
  • SNARE

Cite this

Weber-Boyvat, Marion ; Chernov, Konstantin G. ; Aro, Nina ; Wohlfahrt, Gerd ; Okkkonen, Vesa M. ; Jäntti, Jussi. / The Sec1/Munc18 protein groove plays a conserved role in interaction with Sec9p/SNAP-25. In: Traffic. 2016 ; Vol. 17, No. 2. pp. 131-153.
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abstract = "The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNAREmediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here we show that a sec1 groove mutant yeast strain, sec1(w24), displays temperature sensitive growth and secretion defects. The yeast Sec1p and mammalian Munc18-1 grooves were shown to play an important role in the interaction with the SNAREs Sec9p and SNAP-25b, respectively. Incubation of SNAP-25b with Munc18-1 groove mutant resulted in a lag in the kinetics of SNARE complex assembly in vitro as compared to wild-type Munc18-1. The SNARE regulator SRO7 was identified as a multicopy suppressor of sec1(w24) groove mutant and an intact Sec1p groove was required for the plasma membrane targeting of Sro7p-SNARE complexes. Simultaneous inactivation of Sec1p groove and SRO7 resulted in reduced levels of exocytic SNARE complexes. Our results identify the groove as a conserved interaction surface in SM proteins. The results indicate that this structural element is important for interactions with Sec9p/SNAP-25 and participates, in concert with Sro7p, in the initial steps of SNARE complex assembly.",
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author = "Marion Weber-Boyvat and Chernov, {Konstantin G.} and Nina Aro and Gerd Wohlfahrt and Okkkonen, {Vesa M.} and Jussi J{\"a}ntti",
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The Sec1/Munc18 protein groove plays a conserved role in interaction with Sec9p/SNAP-25. / Weber-Boyvat, Marion (Corresponding Author); Chernov, Konstantin G.; Aro, Nina; Wohlfahrt, Gerd; Okkkonen, Vesa M.; Jäntti, Jussi (Corresponding Author).

In: Traffic, Vol. 17, No. 2, 2016, p. 131-153.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The Sec1/Munc18 protein groove plays a conserved role in interaction with Sec9p/SNAP-25

AU - Weber-Boyvat, Marion

AU - Chernov, Konstantin G.

AU - Aro, Nina

AU - Wohlfahrt, Gerd

AU - Okkkonen, Vesa M.

AU - Jäntti, Jussi

PY - 2016

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N2 - The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNAREmediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here we show that a sec1 groove mutant yeast strain, sec1(w24), displays temperature sensitive growth and secretion defects. The yeast Sec1p and mammalian Munc18-1 grooves were shown to play an important role in the interaction with the SNAREs Sec9p and SNAP-25b, respectively. Incubation of SNAP-25b with Munc18-1 groove mutant resulted in a lag in the kinetics of SNARE complex assembly in vitro as compared to wild-type Munc18-1. The SNARE regulator SRO7 was identified as a multicopy suppressor of sec1(w24) groove mutant and an intact Sec1p groove was required for the plasma membrane targeting of Sro7p-SNARE complexes. Simultaneous inactivation of Sec1p groove and SRO7 resulted in reduced levels of exocytic SNARE complexes. Our results identify the groove as a conserved interaction surface in SM proteins. The results indicate that this structural element is important for interactions with Sec9p/SNAP-25 and participates, in concert with Sro7p, in the initial steps of SNARE complex assembly.

AB - The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNAREmediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here we show that a sec1 groove mutant yeast strain, sec1(w24), displays temperature sensitive growth and secretion defects. The yeast Sec1p and mammalian Munc18-1 grooves were shown to play an important role in the interaction with the SNAREs Sec9p and SNAP-25b, respectively. Incubation of SNAP-25b with Munc18-1 groove mutant resulted in a lag in the kinetics of SNARE complex assembly in vitro as compared to wild-type Munc18-1. The SNARE regulator SRO7 was identified as a multicopy suppressor of sec1(w24) groove mutant and an intact Sec1p groove was required for the plasma membrane targeting of Sro7p-SNARE complexes. Simultaneous inactivation of Sec1p groove and SRO7 resulted in reduced levels of exocytic SNARE complexes. Our results identify the groove as a conserved interaction surface in SM proteins. The results indicate that this structural element is important for interactions with Sec9p/SNAP-25 and participates, in concert with Sro7p, in the initial steps of SNARE complex assembly.

KW - exocytosis

KW - Sec1

KW - Munc18

KW - Sec9

KW - SNAP-25

KW - Sro7

KW - Tomosyn

KW - SNARE

U2 - 10.1111/tra.12349

DO - 10.1111/tra.12349

M3 - Article

VL - 17

SP - 131

EP - 153

JO - Traffic

JF - Traffic

SN - 1398-9219

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