Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p (Q37213774)

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scientific article published on 16 August 2013

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English	Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p	scientific article published on 16 August 2013

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p (English)

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

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author name string

Vidya Karunakaran

1

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

William Wickner

2

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Europe PubMed Central

PMC publication ID

19 August 2017

language of work or name

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publication date

16 August 2013

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Europe PubMed Central

PMC publication ID

19 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

PMC publication ID

19 August 2017

288

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Europe PubMed Central

PMC publication ID

19 August 2017

40

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

28557-28566

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release

1 reference

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Membrane fusion catalyzed by a Rab, SNAREs, and SNARE chaperones is accompanied by enhanced permeability to small molecules and by lysis

1 reference

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HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly

1 reference

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Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components

1 reference

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Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion

1 reference

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Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusion

1 reference

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6 September 2017

The major role of the Rab Ypt7p in vacuole fusion is supporting HOPS membrane association

1 reference

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Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones

1 reference

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Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification.

1 reference

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Rab cascades and tethering factors in the endomembrane system

1 reference

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Reversible, cooperative reactions of yeast vacuole docking

1 reference

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Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p

1 reference

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The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p

1 reference

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Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles

1 reference

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Diacylglycerol and its formation by phospholipase C regulate Rab- and SNARE-dependent yeast vacuole fusion

1 reference

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Sec1p directly stimulates SNARE-mediated membrane fusion in vitro

1 reference

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A soluble SNARE drives rapid docking, bypassing ATP and Sec17/18p for vacuole fusion.

1 reference

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Trans-SNARE interactions elicit Ca2+ efflux from the yeast vacuole lumen

1 reference

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A cycle of Vam7p release from and PtdIns 3-P-dependent rebinding to the yeast vacuole is required for homotypic vacuole fusion

1 reference

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Ergosterol is required for the Sec18/ATP-dependent priming step of homotypic vacuole fusion

1 reference

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Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

1 reference

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Sequential action of two GTPases to promote vacuole docking and fusion

1 reference

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A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion

1 reference

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Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion

1 reference

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Sec1p binds to SNARE complexes and concentrates at sites of secretion

1 reference

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Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

1 reference

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Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

1 reference

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Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion

1 reference

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1 reference

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Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)

1 reference

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SNAP receptors implicated in vesicle targeting and fusion

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G-protein ligands inhibit in vitro reactions of vacuole inheritance

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The GTPase Ypt7p of Saccharomyces cerevisiae is required on both partner vacuoles for the homotypic fusion step of vacuole inheritance.

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Use of resonance energy transfer to monitor membrane fusion

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1 reference

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12 December 2020

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Identifiers

10.1074/JBC.M113.484410

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

19 August 2017

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