Elsevier

Experimental Cell Research

Volume 271, Issue 1, 15 November 2001, Pages 10-21
Experimental Cell Research

Minireview
SNARE Complex Structure and Function

https://doi.org/10.1006/excr.2001.5368Get rights and content

First page preview

First page preview
Click to open first page preview

References (101)

  • R. Laage et al.

    A conserved membrane-spanning amino acid motif drives homomeric and supports heteromeric assembly of presynaptic SNARE proteins

    J. Biol. Chem.

    (2000)
  • R.R. Gerona et al.

    The C terminus of SNAP-25 is essential for ca(2+)-dependent binding of synaptotagmin to SNARE complexes

    J. Biol. Chem.

    (2000)
  • H. Tokumaru et al.

    SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis

    Cell

    (2001)
  • I. Fernandez et al.

    Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1a

    Cell

    (1998)
  • L.C. Gonzalez et al.

    A novel SNARE N-terminal domain revealed by the crystal structure of sec22b

    J. Biol. Chem.

    (2001)
  • J.C. Hay et al.

    SNAREs and NSF in targeted membrane fusion

    Curr. Opin. Cell Biol.

    (1997)
  • D. Chen et al.

    Molecular mechanisms of platelet exocytosis: Role of SNAP-23 and syntaxin 2 in dense core granule release

    Blood

    (2000)
  • J. Min et al.

    Synip: A novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes

    Mol. Cell

    (1999)
  • R. Flaumenhaft et al.

    Proteins of the exocytotic core complex mediate platelet alpha-granule secretion. Roles of vesicle-associated membrane protein, SNAP-23, and syntaxin 4

    J. Biol. Chem.

    (1999)
  • S.H. Wong et al.

    Syntaxin 7, a novel syntaxin family member associated with the early endosomal compartment

    J. Biol. Chem.

    (1998)
  • R. Prekeris et al.

    Syntaxin 11 is an atypical SNARE abundant in the immune system

    Eur. J. Cell Biol.

    (2000)
  • B.L. Tang et al.

    Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins

    Biochem. Biophys. Res. Commun.

    (1998)
  • A. Simonsen et al.

    Syntaxin-16, a putative Golgi t-SNARE

    Eur. J. Cell Biol.

    (1998)
  • K. Hatsuzawa et al.

    Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking

    J. Biol. Chem.

    (2000)
  • Y. Xu et al.

    A 29-kilodalton Golgi soluble n-ethylmaleimide-sensitive factor attachment protein receptor (vti1-rp2) implicated in protein trafficking in the secretory pathway

    J. Biol. Chem.

    (1998)
  • A. Charest et al.

    Association of a novel pdz domain-containing peripheral Golgi protein with the Q-SNARE protein syntaxin 6

    J. Biol. Chem.

    (2001)
  • B. Martin-Martin et al.

    Involvement of SNAP-23 and syntaxin 6 in human neutrophil exocytosis

    Blood

    (2000)
  • A. Simonsen et al.

    The rab5 effector EEA1 interacts directly with syntaxin-6

    J. Biol. Chem.

    (1999)
  • B.L. Tang et al.

    Syntaxin 10: A member of the syntaxin family localized to the trans-Golgi network

    Biochem. Biophys. Res. Commun.

    (1998)
  • Y. Xu et al.

    Gs15, a 15-kilodalton Golgi soluble n-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbet1

    J. Biol. Chem.

    (1997)
  • H.Y. Gaisano et al.

    SNAP-23 is located in the basolateral plasma membrane of rat pancreatic acinar cells

    FEBS Lett.

    (1997)
  • S.M. Leung et al.

    SNAP-23 requirement for transferrin recycling in streptolysin-O- permeabilized Madin–Darby canine kidney cells

    J. Biol. Chem.

    (1998)
  • Z. Guo et al.

    Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells

    Cell

    (1998)
  • M. Steegmaier et al.

    Three novel proteins of the syntaxin/SNAP-25 family

    J. Biol. Chem.

    (1998)
  • T. Zhang et al.

    Ykt6 forms a SNARE complex with syntaxin 5, GS28 and bet1 and participates in a late stage in ER–Golgi transport

    J. Biol. Chem.

    (2001)
  • Y. Fujita et al.

    Tomosyn: A syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process

    Neuron

    (1998)
  • R.B. Sutton et al.

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

    Nature

    (1998)
  • M.A. Poirier et al.

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

    Nat. Struct. Biol.

    (1998)
  • J.A. McNew et al.

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

    J. Cell Biol.

    (2000)
  • T. Sollner et al.

    SNAP receptors implicated in vesicle targeting and fusion

    Nature

    (1993)
  • W. Nickel et al.

    Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs

    Proc. Natl. Acad. Sci. USA

    (1999)
  • C. Ungermann et al.

    Defining the functions of trans-SNARE pairs

    Nature

    (1998)
  • C. Peters et al.

    Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion

    Nature

    (2001)
  • J.A. McNew et al.

    Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

    Nature

    (2000)
  • S.Y. Hua et al.

    Activity-dependent changes in partial VAMP complexes during neurotransmitter release

    Nat. Neurosci.

    (1999)
  • M.G. Waters et al.

    Membrane tethering and fusion in the secretory and endocytic pathways

    Traffic

    (2000)
  • J.B. Bock et al.

    A genomic perspective on membrane compartment organization

    Nature

    (2001)
  • R. Fukuda et al.

    Functional architecture of an intracellular membrane t-SNARE

    Nature

    (2000)
  • W. Antonin et al.

    A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function

    EMBO J.

    (2000)
  • D. Fasshauer et al.

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

    Proc. Natl. Acad. Sci. USA

    (1998)
  • Cited by (83)

    • Soybean Golgi SNARE 12 protein interacts with Soybean mosaic virus encoded P3N-PIPO protein

      2016, Biochemical and Biophysical Research Communications
      Citation Excerpt :

      Therefore, the potyvirus P3N-PIPO has been suggested as the classical movement protein (MP) [6,7]. soluble N-ethyl-maleimide-sensitive-factor attachment protein receptors (SNAREs) are small proteins (18–42 kDa) containing cytoplasmic amphipathic helices, referred to as SNARE motifs, that engage in pernicious coiled coil interactions with other SNAREs [8]. In eukaryotic cells, specific membrane fusion between transport vesicles and target membranes is mediated by the SNARE complex that assembles into a tight cluster of four coiled-coil helices [9–12].

    • Orchestrating Lymphocyte Polarity in Cognate Immune Cell–Cell Interactions

      2016, International Review of Cell and Molecular Biology
      Citation Excerpt :

      Specifically, vesicles carry specific vesicle (v-) SNARE and target membranes contain target (t-) SNAREs. Vesicle docking and priming is enabled by the formation of a complex between two t-SNAREs (syntaxin-3 or -4 and SNAP-23 in nonneuronal cells) and one v-SNARE, for example, VAMP3 (Hay, 2001). This process requires the presence of high Ca2+ (Hay, 2001) and depends on MTs (Beemiller et al., 2012).

    View all citing articles on Scopus
    1

    To whom correspondence and reprint requests should be addressed. Fax: 734 647 0884. E-mail: [email protected].

    View full text