Identification of SNAP-47, a Novel Qbc-SNARE with Ubiquitous Expression*

The SNARE proteins are essential components of the intracellular fusion machinery. It is thought that they form a tight four-helix complex between membranes, in effect initiating fusion. Most SNAREs contain a single coiled-coil region, referred to as the SNARE motif, directly adjacent to a single transmembrane domain. The neuronal SNARE SNAP-25 defines a subfamily of SNARE proteins with two SNARE helices connected by a longer linker, comprising also the proteins SNAP-23 and SNAP-29. We now report the initial characterization of a novel vertebrate homologue termed SNAP-47. Northern blot and immunoblot analysis revealed ubiquitous tissue distribution, with particularly high levels in nervous tissue. In neurons, SNAP-47 shows a widespread distribution on intracellular membranes and is also enriched in synaptic vesicle fractions. In vitro, SNAP-47 substituted for SNAP-25 in SNARE complex formation with the neuronal SNAREs syntaxin 1a and synaptobrevin 2, and it also substituted for SNAP-25 in proteoliposome fusion. However, neither complex assembly nor fusion was as efficient as with SNAP-25.

[1]  T. Dresbach,et al.  Synaptic targeting of neuroligin is independent of neurexin and SAP90/PSD95 binding , 2004, Molecular and Cellular Neuroscience.

[2]  C. Seidel,et al.  Determinants of liposome fusion mediated by synaptic SNARE proteins. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[3]  Robert C. Edgar,et al.  MUSCLE: multiple sequence alignment with high accuracy and high throughput. , 2004, Nucleic acids research.

[4]  Dirk Fasshauer,et al.  A Transient N-terminal Interaction of SNAP-25 and Syntaxin Nucleates SNARE Assembly* , 2004, Journal of Biological Chemistry.

[5]  J. Bonifacino,et al.  The Mechanisms of Vesicle Budding and Fusion , 2004, Cell.

[6]  Nils Brose,et al.  A Family of Ca2+-Dependent Activator Proteins for Secretion , 2003, Journal of Biological Chemistry.

[7]  Charles Barlowe,et al.  Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function. , 2002, Molecular biology of the cell.

[8]  E. McCarthy,et al.  Plasma membrane targeting of SNAP-25 increases its local concentration and is necessary for SNARE complex formation and regulated exocytosis. , 2002, Journal of cell science.

[9]  R. Flaumenhaft,et al.  Subcellular distribution of 3 functional platelet SNARE proteins: human cellubrevin, SNAP-23, and syntaxin 2. , 2002, Blood.

[10]  V. Subramaniam,et al.  SNARE assembly and disassembly exhibit a pronounced hysteresis , 2002, Nature Structural Biology.

[11]  W. Antonin,et al.  Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs , 2002, Nature Structural Biology.

[12]  B. Giros,et al.  The Existence of a Second Vesicular Glutamate Transporter Specifies Subpopulations of Glutamatergic Neurons , 2001, The Journal of Neuroscience.

[13]  P. Washbourne,et al.  Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. , 2001, The Biochemical journal.

[14]  R. Jahn,et al.  Homo- and Heterooligomeric SNARE Complexes Studied by Site-directed Spin Labeling* , 2001, The Journal of Biological Chemistry.

[15]  Andrew A. Peden,et al.  A genomic perspective on membrane compartment organization , 2001, Nature.

[16]  Richard H. Scheller,et al.  SNARE-mediated membrane fusion , 2001, Nature Reviews Molecular Cell Biology.

[17]  Noam E Ziv,et al.  Assembly of New Individual Excitatory Synapses Time Course and Temporal Order of Synaptic Molecule Recruitment , 2000, Neuron.

[18]  G. Schiavo,et al.  Neurotoxins affecting neuroexocytosis. , 2000, Physiological reviews.

[19]  C. McBain,et al.  Snap-25 is polarized to axons and abundant along the axolemma: an immunogold study of intact neurons , 2000, Journal of neurocytology.

[20]  W. Antonin,et al.  Mixed and Non-cognate SNARE Complexes , 1999, The Journal of Biological Chemistry.

[21]  R. Scheller,et al.  SNARE Interactions Are Not Selective , 1999, The Journal of Biological Chemistry.

[22]  N. Brose,et al.  Differential expression of two novel Munc13 proteins in rat brain. , 1999, The Biochemical journal.

[23]  S. Wong,et al.  GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with syntaxin 6. , 1999, Molecular biology of the cell.

[24]  A. Brunger,et al.  Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[25]  R. Scheller,et al.  Three Novel Proteins of the Syntaxin/SNAP-25 Family* , 1998, The Journal of Biological Chemistry.

[26]  T. Weimbs,et al.  A model for structural similarity between different SNARE complexes based on sequence relationships. , 1998, Trends in cell biology.

[27]  T. Shirao,et al.  Differential expression of rat brain synaptic proteins in development and aging. , 1998, Biochemical and biophysical research communications.

[28]  Reinhard Jahn,et al.  Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution , 1998, Nature.

[29]  A. T. Brunger,et al.  Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. , 1998, Biochemistry.

[30]  Benedikt Westermann,et al.  SNAREpins: Minimal Machinery for Membrane Fusion , 1998, Cell.

[31]  Reinhard Jahn,et al.  Structure and Conformational Changes in NSF and Its Membrane Receptor Complexes Visualized by Quick-Freeze/Deep-Etch Electron Microscopy , 1997, Cell.

[32]  P. Scherer,et al.  Syndet is a novel SNAP-25 related protein expressed in many tissues. , 1997, Journal of cell science.

[33]  R. Jahn,et al.  16-BAC/SDS-PAGE: a two-dimensional gel electrophoresis system suitable for the separation of integral membrane proteins. , 1996, Analytical biochemistry.

[34]  T. Südhof,et al.  Fatty acylation of synaptotagmin in PC12 cells and synaptosomes. , 1996, Biochemical and biophysical research communications.

[35]  P. Roche,et al.  Identification of a Novel Syntaxin- and Synaptobrevin/VAMP-binding Protein, SNAP-23, Expressed in Non-neuronal Tissues* , 1996, The Journal of Biological Chemistry.

[36]  A. Shevchenko,et al.  Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. , 1996, Analytical chemistry.

[37]  D. Storm,et al.  Analysis of the palmitoylation and membrane targeting domain of neuromodulin (GAP-43) by site-specific mutagenesis. , 1993, Biochemistry.

[38]  N. Düzgüneş,et al.  Lipid mixing assays to determine fusion in liposome systems. , 1993, Methods in enzymology.

[39]  J. Skene,et al.  The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS , 1992, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[40]  P. De Camilli,et al.  P29: a novel tyrosine-phosphorylated membrane protein present in small clear vesicles of neurons and endocrine cells , 1990, The Journal of cell biology.

[41]  H. Okayama,et al.  High-efficiency transformation of mammalian cells by plasmid DNA. , 1987, Molecular and cellular biology.

[42]  P. Greengard,et al.  Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation , 1983, The Journal of cell biology.