The specificity of SNARE-dependent fusion is encoded in the SNARE motif (Q27932181)

Tlg1p YDR468C

1 reference

SNAP receptor SNC2 YOR327C

1 reference

SNAP receptor PEP12 YOR036W

1 reference

Proceedings of the National Academy of Sciences of the United States of America

Fabienne Paumet

1

Fabienne

Paumet

1 reference

21 October 2023

Vahid Rahimian

series ordinal

2

author given names

Vahid

author last names

Rahimian

1 reference

21 October 2023

James E Rothman

series ordinal

3

author given names

James E

author last names

Rothman

1 reference

21 October 2023

language of work or name

English

0 references

publication date

9 March 2004

0 references

published in

1 reference

1 December 2016

101

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issue

10

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page(s)

3376-80

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cites work

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Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog

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Distinct SNARE complexes mediating membrane fusion in Golgi transport based on combinatorial specificity

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Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

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A t-SNARE of the endocytic pathway must be activated for fusion.

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An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p

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A novel snare N-terminal domain revealed by the crystal structure of Sec22b

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Vam3p structure reveals conserved and divergent properties of syntaxins

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Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly

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Topological restriction of SNARE-dependent membrane fusion

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Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

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SNAREs contribute to the specificity of membrane fusion

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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

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Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport.

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Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures

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Two syntaxin homologues in the TGN/endosomal system of yeast

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Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae

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The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p

20 March 2017

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A conserved domain is present in different families of vesicular fusion proteins: a new superfamily

20 March 2017

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Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast

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Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae.

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SNAREpins: minimal machinery for membrane fusion

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The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly

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SNARE Protein Structure and Function

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Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins.

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What is the role of SNARE proteins in membrane fusion?

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Regulation of membrane fusion by the membrane-proximal coil of the t-SNARE during zippering of SNAREpins

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Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors

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Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain

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The synaptic SNARE complex is a parallel four-stranded helical bundle

21 January 2018

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A genomic perspective on membrane compartment organization.

21 January 2018

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Functional architecture of an intracellular membrane t-SNARE

21 January 2018

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Liposome fusion assay to monitor intracellular membrane fusion machines

21 January 2018

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Pep12p is a multifunctional yeast syntaxin that controls entry of biosynthetic, endocytic and retrograde traffic into the prevacuolar compartment

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21 January 2018

Identifiers

DOI

10.1073/PNAS.0400271101

1 reference

3374762

ADS bibcode

2004PNAS..101.3376P

0 references

3374762

1 reference

1 reference

1 reference