Biology:SNAP25

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example


Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans.[1][2] SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.[3]

Structure and function

Molecular machinery driving exocytosis in neuromediator release. The core SNARE complex is formed by four α-helices contributed by synaptobrevin, syntaxin and SNAP-25. Synaptotagmin serves as a Ca2+ sensor and intimately regulates SNARE zipping.[4]

SNAP-25, a Q-SNARE protein, is anchored to the cytosolic face of membranes via palmitoyl side chains covalently bound to cysteine amino acid residues in the central linker domain of the molecule. This means that SNAP-25 does not contain a trans-membrane domain.[5]

SNAP-25 has been identified to contribute two[6] α-helices to the SNARE complex, a four-α-helix domain complex.[7] The SNARE complex participates in vesicle fusion, which involves the docking, priming and merging of a vesicle with the cell membrane to initiate an exocytotic event. Synaptobrevin, a protein that is a part of the vesicle-associated membrane protein (VAMP) family, and syntaxin-1 also help form the SNARE complex by each contributing a single α-helix. SNAP-25 assembles with synaptobrevin and syntaxin-1, and the selective binding of these proteins enables vesicle docking and fusion to occur at active zones on the plasma membrane.[8] The energy needed for fusion to occur, results from the assembly of the SNARE proteins along with additional Sec1/Munc18-like (SM) proteins.[9]

To form the SNARE complex, synaptobrevin, syntaxin-1, and SNAP-25 associate and begin to wrap around each other to form a coiled coil quaternary structure. The α-helices of both synaptobrevin and syntaxin-1 bind to those of SNAP-25. Synaptobrevin binds the α-helix near the C-terminus of SNAP-25, while syntaxin-1 binds the α-helix near the N-terminus.[5] Dissociation of the SNARE complex is driven by ATPase N-ethylmaleimide-sensitive fusion (NSF) protein.[9]

SNAP-25 inhibits presynaptic P-, Q-, and L-type voltage-gated calcium channels[10] and interacts with the synaptotagmin C2B domain in a Ca2+-independent fashion.[11] In glutamatergic synapses, SNAP-25 decreases the Ca2+ responsiveness, while it is normally absent in GABAergic synapses.[12]

Two isoforms (mRNA splice variants) of SNAP-25 exist, which are SNAP-25a and SNAP-25b. The two isoforms differ by nine amino acid residues, including a re-localization of one of the four palmitoylated cysteine residues involved in membrane attachment.[13] The major characteristics of these two forms are outlined in the table below.

SNAP25a SNAP25b
Structure N-terminal α-helix

Random coil linker region with four cysteines clustered towards the center

C-terminal α-helix

N-terminal α-helix

Random coil linker region with four cysteines clustered towards the C-terminus

C-terminal α-helix

Expression Major SNAP-25 isoform in embryos and developing neural tissue

Minimal expression in adult tissue except in pituitary and adrenal gland tissues

Minimal expression during development, major isoform in adult neural tissue[14]
Localization Diffuse Localized to terminals and varicosities[14]

SNAP-25 not only plays a role in synaptogenesis and the exocytotic release of neurotransmitters, but it also affects spine morphogenesis and density, post synaptic receptor trafficking and neuronal plasticity. Other non-neuronal processes such as metabolism can also be affected by SNAP-25 protein expression.[15][16]

Clinical significance

Developmental and epileptic encephalopathies (DEEs)

Individuals harboring pathogenic heterozygous de novo missense or loss-of-function variants in SNAP-25 often present with an early-onset developmental and epileptic encephalopathy. The core symptoms comprise intellectual disability ranging between mild to profound and early-onset seizures mostly occurring before the age of two years. Further recurrent symptoms include movement disorders, cerebral visual impairment, and brain atrophy.[17] Electrophysiological studies identified aberrant spontaneous neurotransmission as causative and suggest that structurally clustered pathogenic variants lead to similar synaptic phenotypes.[18]

Attention Deficit Hyperactivity Disorder (ADHD)

Consistent with the regulation of synaptic Ca2+ responsiveness, heterozygous deletion of the SNAP-25 gene in mice results in a hyperactive phenotype similar to attention deficit hyperactivity disorder (ADHD). In heterozygous mice, a decrease in hyperactivity is observed with dextroamphetamine (or Dexedrine), an active ingredient in the ADHD drug Adderall. Homozygous deletions of the SNAP-25 gene are lethal. An additional study indicated that incorporation of a SNAP-25 transgene back into the heterozygous SNAP-25 mutant mouse can rescue normal activity levels similar to wildtype mice. This suggests that low protein levels of SNAP-25 can be a cause of hyper-kinetic behavior.[19] Subsequent studies have suggested that at least some of the SNAP-25 gene mutations in humans might predispose to ADHD.[20][21] Identification of polymorphisms in the 3’ untranslated region of the SNAP-25 gene was established in linkage studies with families that had been pre-diagnosed ADHD.[22]

Schizophrenia

Studies in the post mortem brains of patients with Schizophrenia have shown that altered protein levels of SNAP-25 are specific to regions of the brain. Reduced SNAP-25 protein expression has been observed in the hippocampus as well as an area of the frontal lobe known as Broadman’s area 10 whereas SNAP-25 expression has increased in both the cingulate cortex and prefrontal lobe of Broadman’s area 9. The varying levels of SNAP-25 protein found in different areas of the brain have been thought to contribute to the conflicting psychological behaviors (depressive vs. hyperactive) expressed in some Schizophrenic patients.[23][24][25][26]

The blind-drunk (Bdr) mouse model which has a point mutations in the SNAP-25b protein has provided a complex phenotype involving behaviors such as an abnormal circadian rhythm,[27] uncoordinated gait, and disinterest in new objects/toys.[28] Another mouse model generated from Cre-LoxP recombination, showed that conditional knockout (cKO) of the SNAP-25 gene in the forebrain, showed inactive SNAP-25 gene expression in glutamatergic neurons. However, significant glutamate levels were found in the cortex of these cKO mice.[29] These mice also exhibited deficient social skills, impaired learning and memory, enhanced kinesthetic activity, a reduced startle response, impaired self-care, nursing ability and nest-building skills. Antipsychotic drugs such as Clozapine and Riluzole have been shown to significantly reduce the schizophrenic phenotype expressed in SNAP-25 cKO mice.[29]

Alzheimer's disease

Individuals with Alzhiemer’s disease have been shown to have decreased presynaptic protein levels and impaired synaptic function in neurons. SNAP-25 can be used as a biomarker in the cerebral spinal fluid (CSF) of patients exhibiting different variations of Alzheimer's disease (prodromal Alzheimer’s and overt Alzheimer’s). Increased levels of SNAP-25 protein were observed in patients with Alzheimer’s compared to control individuals. Additionally, the presence of truncated SNAP-25 protein can be seen in the CSF of some patients with this disease. [30] In five distinct regions of the brain, low levels of SNAP-25 can be seen in patients with Alzheimer’s.[31]

Bipolar disorder

A single nucleotide polymorphism in the SNAP-25 gene promoter has been shown to influence the expression levels of the SNAP-25b isoform in the prefrontal cortex. Increased levels of SNAP-25b have been shown to impair synaptic transmission and maturation which could lead to early-onset bipolar disorder (EOBD).The most abundant isoform of SNAP-25 is SNAP-25a during the early weeks of development in mice however in adulthood there is a change and the SNAP-25b isoform increases in the brain. This is shown to correlate with adolescent humans being increasingly diagnosed with EOBD during puberty.[32] It has been suggested that early-onset bipolar disorder is more closely linked to Schizophrenia than to Bipolar Disorder itself. The single nucleotide polymorphism of SNAP-25 (rs6039769) associated with EOBD has been shown to increase the risk of patients developing Schizophrenia.[15]

Botulism

A genome wide association study pointed to the rs362584 polymorphism in the gene as possibly associated with the personality trait neuroticism.[33] Botulinum toxins A, C and E cleave SNAP-25,[34] leading to paralysis in clinically developed botulism.

Epilepsy

Deletion of the SNAP-25b isoform has been shown to cause developmental abnormalities and seizures in mice. High levels of SNAP-25a and the protein syntaxin appear to be linked to seizures found in infantile-epilepsy. SNAP-25 knock-in mice have distinct phenotypic behavior similar to the fits and seizures of epileptic patients, as well as anxiety.[35]

Learning disabilities

In the coloboma hyperactive mutant mouse model where SNAP-25 protein levels are reduced to 50% of the normal level, depolarized neurotransmitter release of dopamine and serotonin were reduced as well as glutamate release. The reduction in glutamate levels can lead to deficient memory and increased learning disabilities.[36] Certain polymorphisms of SNAP-25 (rs363043, rs353016, rs363039, rs363050) have been shown to affect the cognitive behavior, specifically the Intelligence Quotient (IQ)), of patients without pre-existing neurological diseases.[37]

Neonatal development

SNAP-25 protein expression can be altered by sex hormone levels in neonatal rats. Male rats that received an antiestrogen drug showed a 30% decrease in SNAP-25 levels and females treated with estrogen or testosterone showed a 30% increase in SNAP-25 levels.[38] This suggests that synaptosomal proteins, such as SNAP-25, may have a dependence on neonatal hormone levels during brain development in rats. An additional study, showed that SNAP-25 levels in the hippocampus of the brain in neonatal mice were altered if the mother had been exposed to human influenza virus during pregnancy.[39]

Impact in other non-humans

Loss is lethal to Drosophila, but can be fully substituted by overexpression of the related SNAP-24.[6]

Interactive pathway map

Interactions

SNAP-25 has been shown to interact with:


References

  1. ↑ "Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p)". Mammalian Genome 7 (5): 400–1. May 1996. doi:10.1007/s003359900120. PMID 8661740. 
  2. ↑ "SNAP-25 in Major Psychiatric Disorders: A Review". Neuroscience. SNARE Proteins: A Long Journey of Science in Brain Health and Disease 420: 79–85. November 2019. doi:10.1016/j.neuroscience.2019.02.008. PMID 30790667. 
  3. ↑ "Snares and Munc18 in synaptic vesicle fusion". Nature Reviews. Neuroscience 3 (8): 641–53. August 2002. doi:10.1038/nrn898. PMID 12154365. 
  4. ↑ "Subneuronal processing of information by solitary waves and stochastic processes". Nano and Molecular Electronics Handbook. Nano and Microengineering Series. CRC Press. 2007. pp. 17–1–17–41. doi:10.1201/9781315221670. ISBN 978-0-8493-8528-5. https://www.taylorfrancis.com/chapters/edit/10.1201/9781315221670-17/subneuronal-processing-information-solitary-waves-stochastic-processes-danko-georgiev-james-glazebrook. 
  5. ↑ 5.0 5.1 "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils". The Journal of Biological Chemistry 269 (44): 27427–32. November 1994. doi:10.1016/S0021-9258(18)47003-2. PMID 7961655. 
  6. ↑ 6.0 6.1 6.2 "SNARE protein structure and function". Annual Review of Cell and Developmental Biology (Annual Reviews) 19 (1): 493–517. 2003. doi:10.1146/annurev.cellbio.19.110701.155609. PMID 14570579. 
  7. ↑ "Specificity and regulation of a synaptic vesicle docking complex". Neuron 13 (2): 353–61. August 1994. doi:10.1016/0896-6273(94)90352-2. PMID 8060616. 
  8. ↑ "Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking". Science 263 (5150): 1146–9. February 1994. doi:10.1126/science.8108733. PMID 8108733. Bibcode: 1994Sci...263.1146C. 
  9. ↑ 9.0 9.1 "Synaptic vesicle exocytosis". Cold Spring Harbor Perspectives in Biology 3 (12): a005637. December 2011. doi:10.1101/cshperspect.a005637. PMID 22026965. 
  10. ↑ "SNAP-25". The International Journal of Biochemistry & Cell Biology 30 (10): 1069–73. October 1998. doi:10.1016/S1357-2725(98)00079-X. PMID 9785471. 
  11. ↑ "Synaptotagmin: a Ca(2+) sensor that triggers exocytosis?". Nature Reviews. Molecular Cell Biology 3 (7): 498–508. July 2002. doi:10.1038/nrm855. PMID 12094216. http://www.physiology.wisc.edu/chapman/papers/naturereview.pdf. 
  12. ↑ "SNAP-25 modulation of calcium dynamics underlies differences in GABAergic and glutamatergic responsiveness to depolarization". Neuron 41 (4): 599–610. February 2004. doi:10.1016/S0896-6273(04)00077-7. PMID 14980208. 
  13. ↑ "Alternative splicing of SNAP-25 regulates secretion through nonconservative substitutions in the SNARE domain". Molecular Biology of the Cell 16 (12): 5675–85. December 2005. doi:10.1091/mbc.E05-07-0595. PMID 16195346. 
  14. ↑ 14.0 14.1 "Differential expression of SNAP-25 protein isoforms during divergent vesicle fusion events of neural development". Proceedings of the National Academy of Sciences of the United States of America 92 (5): 1510–4. February 1995. doi:10.1073/pnas.92.5.1510. PMID 7878010. Bibcode: 1995PNAS...92.1510B. 
  15. ↑ 15.0 15.1 "SNAP25 At-Risk Variant for Bipolar Disorder and Schizophrenia". The Journal of Neuroscience 37 (43): 10389–10397. October 2017. doi:10.1523/JNEUROSCI.1040-17.2017. PMID 28972123. 
  16. ↑ "SNAP-25, a Known Presynaptic Protein with Emerging Postsynaptic Functions" (in en). Frontiers in Synaptic Neuroscience 8: 7. 2016. doi:10.3389/fnsyn.2016.00007. PMID 27047369. 
  17. ↑ "De novo variants in SNAP25 cause an early-onset developmental and epileptic encephalopathy". Genetics in Medicine 23 (4): 653–660. April 2021. doi:10.1038/s41436-020-01020-w. PMID 33299146. https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=60808. 
  18. ↑ "Role of Aberrant Spontaneous Neurotransmission in SNAP25-Associated Encephalopathies". Neuron 109 (1): 59–72.e5. January 2021. doi:10.1016/j.neuron.2020.10.012. PMID 33147442. 
  19. ↑ "Transgenic rescue of SNAP-25 restores dopamine-modulated synaptic transmission in the coloboma mutant". Brain Research 847 (2): 186–95. November 1999. doi:10.1016/S0006-8993(99)02023-5. PMID 10575087. 
  20. ↑ "Synaptosomal-associated protein 25 (SNAP-25) and attention deficit hyperactivity disorder (ADHD): evidence of linkage and association in the Irish population". Molecular Psychiatry 7 (8): 913–7. 2002. doi:10.1038/sj.mp.4001092. PMID 12232787. 
  21. ↑ "Association study of a SNAP-25 microsatellite and attention deficit hyperactivity disorder". American Journal of Medical Genetics 114 (3): 269–71. April 2002. doi:10.1002/ajmg.10253. PMID 11920846. 
  22. ↑ "Identification of DNA variants in the SNAP-25 gene and linkage study of these polymorphisms and attention-deficit hyperactivity disorder". Molecular Psychiatry 5 (4): 405–9. July 2000. doi:10.1038/sj.mp.4000733. PMID 10889551. 
  23. ↑ "SNAP-25 in neuropsychiatric disorders". Annals of the New York Academy of Sciences 1152 (1): 93–9. January 2009. doi:10.1111/j.1749-6632.2008.03995.x. PMID 19161380. Bibcode: 2009NYASA1152...93C. 
  24. ↑ "Increased concentrations of presynaptic proteins in the cingulate cortex of subjects with schizophrenia". Archives of General Psychiatry 54 (6): 559–66. June 1997. doi:10.1001/archpsyc.1997.01830180077010. PMID 9193197. 
  25. ↑ "Altered levels of the synaptosomal associated protein SNAP-25 in schizophrenia". Biological Psychiatry 43 (4): 239–43. February 1998. doi:10.1016/S0006-3223(97)00204-7. PMID 9513732. 
  26. ↑ "SNAP-25 reduction in the hippocampus of patients with schizophrenia". Progress in Neuro-Psychopharmacology & Biological Psychiatry 27 (3): 411–7. May 2003. doi:10.1016/S0278-5846(03)00027-7. PMID 12691775. 
  27. ↑ "Disrupted circadian rhythms in a mouse model of schizophrenia". Current Biology 22 (4): 314–9. February 2012. doi:10.1016/j.cub.2011.12.051. PMID 22264613. 
  28. ↑ "A dominant mutation in Snap25 causes impaired vesicle trafficking, sensorimotor gating, and ataxia in the blind-drunk mouse". Proceedings of the National Academy of Sciences of the United States of America 104 (7): 2431–6. February 2007. doi:10.1073/pnas.0610222104. PMID 17283335. Bibcode: 2007PNAS..104.2431J. 
  29. ↑ 29.0 29.1 "Brain-Specific SNAP-25 Deletion Leads to Elevated Extracellular Glutamate Level and Schizophrenia-Like Behavior in Mice". Neural Plasticity 2017: 4526417. 2017. doi:10.1155/2017/4526417. PMID 29318050. 
  30. ↑ "SNAP-25 is a promising novel cerebrospinal fluid biomarker for synapse degeneration in Alzheimer's disease". Molecular Neurodegeneration 9: 53. November 2014. doi:10.1186/1750-1326-9-53. PMID 25418885. 
  31. ↑ "Decreased levels of synaptosomal associated protein 25 in the brain of patients with Down syndrome and Alzheimer's disease". Electrophoresis 20 (4–5): 928–34. 1999. doi:10.1002/(SICI)1522-2683(19990101)20:4/5<928::AID-ELPS928>3.0.CO;2-Z. PMID 10344268. 
  32. ↑ "A SNAP25 promoter variant is associated with early-onset bipolar disorder and a high expression level in brain". Molecular Psychiatry 15 (7): 748–55. July 2010. doi:10.1038/mp.2008.148. PMID 19125158. 
  33. ↑ "Genome-wide association scan for five major dimensions of personality". Molecular Psychiatry 15 (6): 647–56. June 2010. doi:10.1038/mp.2008.113. PMID 18957941. 
  34. ↑ "Botulinum toxin type A and other botulinum toxin serotypes: a comparative review of biochemical and pharmacological actions". European Journal of Neurology 8 (Suppl 5): 21–9. November 2001. doi:10.1046/j.1468-1331.2001.00035.x. PMID 11851731. 
  35. ↑ "Mutation in SNAP25 as a novel genetic cause of epilepsy and intellectual disability". Rare Diseases 1 (1): e26314. 2013. doi:10.4161/rdis.26314. PMID 25003006. 
  36. ↑ "Coloboma hyperactive mutant mice exhibit regional and transmitter-specific deficits in neurotransmission". Journal of Neurochemistry 68 (1): 176–86. January 1997. doi:10.1046/j.1471-4159.1997.68010176.x. PMID 8978724. 
  37. ↑ "The SNAP-25 gene is associated with cognitive ability: evidence from a family-based study in two independent Dutch cohorts". Molecular Psychiatry 11 (9): 878–86. September 2006. doi:10.1038/sj.mp.4001868. PMID 16801949. https://research.vu.nl/en/publications/ff55aca0-6740-44e1-99bb-79b7dc2d39c5. 
  38. ↑ "Ontogeny, sex dimorphism, and neonatal sex hormone determination of synapse-associated messenger RNAs in rat brain". Brain Research. Molecular Brain Research 20 (1–2): 101–10. October 1993. doi:10.1016/0169-328X(93)90114-5. PMID 8255171. 
  39. ↑ "Differential expression of synaptosome-associated protein 25 kDa [SNAP-25] in hippocampi of neonatal mice following exposure to human influenza virus in utero". Brain Research 800 (1): 1–9. July 1998. doi:10.1016/S0006-8993(98)00450-8. PMID 9685568. 
  40. ↑ 40.0 40.1 40.2 "Three-dimensional structure of the complexin/SNARE complex". Neuron 33 (3): 397–409. January 2002. doi:10.1016/s0896-6273(02)00583-4. PMID 11832227. https://epublications.marquette.edu/cgi/viewcontent.cgi?article=1227&context=chem_fac. 
  41. ↑ "Action of complexin on SNARE complex". The Journal of Biological Chemistry 277 (44): 41652–6. November 2002. doi:10.1074/jbc.M205044200. PMID 12200427. 
  42. ↑ "EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin and SNAP-25. A protein connection between exocytosis and endocytosis?". The Journal of Biological Chemistry 274 (26): 18446–54. June 1999. doi:10.1074/jbc.274.26.18446. PMID 10373452. 
  43. ↑ "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry 41 (50): 14906–15. December 2002. doi:10.1021/bi026417u. PMID 12475239. 
  44. ↑ 44.0 44.1 "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nature Neuroscience 2 (2): 119–24. February 1999. doi:10.1038/5673. PMID 10195194. 
  45. ↑ 45.0 45.1 "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. September 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070. 
  46. ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R. 
  47. ↑ 47.0 47.1 47.2 47.3 "A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic". The Journal of Biological Chemistry 270 (22): 13022–8. June 1995. doi:10.1074/jbc.270.22.13022. PMID 7768895. 
  48. ↑ 48.0 48.1 48.2 48.3 "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues". The Journal of Biological Chemistry 271 (23): 13300–3. June 1996. doi:10.1074/jbc.271.23.13300. PMID 8663154. 
  49. ↑ 49.0 49.1 49.2 "Three novel proteins of the syntaxin/SNAP-25 family". The Journal of Biological Chemistry 273 (51): 34171–9. December 1998. doi:10.1074/jbc.273.51.34171. PMID 9852078. 
  50. ↑ "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal 18 (16): 4372–82. August 1999. doi:10.1093/emboj/18.16.4372. PMID 10449403. 
  51. ↑ "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell 83 (1): 111–9. October 1995. doi:10.1016/0092-8674(95)90239-2. PMID 7553862. 
  52. ↑ "Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells". Journal of Cell Science 113 ( Pt 18) (18): 3197–205. September 2000. doi:10.1242/jcs.113.18.3197. PMID 10954418. https://archive-ouverte.unige.ch/unige:8762. 
  53. ↑ 53.0 53.1 53.2 "Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis". The Journal of Biological Chemistry 276 (44): 40824–33. November 2001. doi:10.1074/jbc.M106141200. PMID 11524423. 
  54. ↑ "SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils". The Journal of Biological Chemistry 269 (44): 27427–32. November 1994. doi:10.1016/S0021-9258(18)47003-2. PMID 7961655. 
  55. ↑ "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: implications for platelet secretion". Blood 93 (8): 2617–26. April 1999. doi:10.1182/blood.V93.8.2617. PMID 10194441. 
  56. ↑ "The C terminus of SNAP25 is essential for Ca(2+)-dependent binding of synaptotagmin to SNARE complexes". The Journal of Biological Chemistry 275 (9): 6328–36. March 2000. doi:10.1074/jbc.275.9.6328. PMID 10692432. 
  57. ↑ "Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis". Neuron 34 (4): 599–611. May 2002. doi:10.1016/s0896-6273(02)00671-2. PMID 12062043. 
  58. ↑ "Effect of mutations in vesicle-associated membrane protein (VAMP) on the assembly of multimeric protein complexes". The Journal of Neuroscience 17 (5): 1596–603. March 1997. doi:10.1523/JNEUROSCI.17-05-01596.1997. PMID 9030619. 

Further reading

External links

This article incorporates text from the public domain Pfam and InterPro: IPR000928



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