Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Abstract Text:

Youngsoo Jun,Hao Xu,Naomi Thorngren,William Wickner,

Intracellular membrane fusion requires SNARE proteins in a trans-complex, anchored to apposed membranes. Proteoliposome studies have suggested that SNAREs drive fusion by stressing the lipid bilayer via their transmembrane domains (TMDs), and that SNARE complexes require a TMD in each docked membrane to promote fusion. Yeast vacuole fusion is believed to require three Q-SNAREs from one vacuole and the R-SNARE Nyv1p from its fusion partner. In accord with this model, we find that fusion is abolished when the TMD of Nyv1p is replaced by lipid anchors, even though lipid-anchored Nyv1p assembles into trans-SNARE complexes. However, normal fusion is restored by the addition of both Sec18p and the soluble SNARE Vam7p. In restoring fusion, Sec18p promotes the disassembly of trans-SNARE complexes, and Vam7p enhances their assembly. Thus, either the TMD of this R-SNARE is not essential for fusion, and TMD-mediated membrane stress is not the only mode of trans-SNARE complex action, or these SNAREs have more flexibility than heretofore appreciated to form alternate functional complexes that violate the 3Q:1R rule.

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Publishing Authors By Initials

Y Jun,H Xu,N Thorngren,W Wickner,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The EMBO journal

VOLUME: 26

Page Numbers: 4935-45

Journal Abbreviation: EMBO J.

ISSN: 1460-2075

DAY: 15

MONTH: 11

YEAR: 2007

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8208664

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.

AFFILIATION: Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3844, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM23377

ACRONYM: GM

MEDLINETA: EMBO J

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion Related Publications

• Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity.
• Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM.
• Excess vacuolar SNAREs drive lysis and Rab bypass fusion.
• HOPS Proofreads the trans-SNARE Complex for Yeast Vacuole Fusion.
• Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones.
• Reversible, cooperative reactions of yeast vacuole docking.
• Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.
• Trans-SNARE complex assembly and yeast vacuole membrane fusion.