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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/07/04 12:54:57」(JST)

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The synapsins are a family of proteins that have long been implicated in the regulation of neurotransmitter release at synapses. Specifically, they are thought to be involved in regulating the number of synaptic vesicles available for release via exocytosis at any one time.^[2]Synapsins are present in invertebrates and vertebrates and are somewhat homologous across evaluated vertebrates.

Current studies suggest the following hypothesis for the role of synapsin: synapsins bind synaptic vesicles to components of the cytoskeleton which prevents them from migrating to the presynaptic membrane and releasing transmitter. During an action potential, synapsins are phosphorylated by PKA (cAMP dependent protein kinase), releasing the synaptic vesicles and allowing them to move to the membrane and release their neurotransmitter.

Gene knockout studies in mice (where the mouse is unable to produce synapsin) have had some surprising results. Mice lacking all three synapsins are prone to seizures, and experience learning defects.^[3] These results suggest that while synapsins are not essential for synaptic function, they do serve an important modulatory role. Conversely, studies using transgenic mice in which neuronal signaling is abolished in specific circuitries showed that synaptic activity regulates, but is not essential to maintain, the expression of these proteins.^[4]

Family members[edit]

Humans and most other vertebrates possess three genes encoding three different synapsin proteins.^[5] Each gene in turn is alternatively spliced to produce at least two different protein isoforms for a total of six isoforms:^[6]

Gene	Protein	Isoforms
SYN1	Synapsin I	Ia, Ib
SYN2	Synapsin II	IIa, IIb
SYN3	Synapsin III	IIIa, IIIb

Different neuron terminals will express varying amounts of each of these synapsin proteins and collectively these synapsins will comprise 1% of the total expressed protein at any one time.^[7] Synapsin Ia has been implicated in bipolar disorder and schizophrenia.^[8]

References[edit]

^ Esser L, Wang CR, Hosaka M, Smagula CS, Südhof TC, Deisenhofer J (February 1998). "Synapsin I is structurally similar to ATP-utilizing enzymes". EMBO J. 17 (4): 977–84. doi:10.1093/emboj/17.4.977. PMC 1170447. PMID 9463376.
^ Evergren E, Benfenati F, Shupliakov O (September 2007). "The synapsin cycle: a view from the synaptic endocytic zone". J. Neurosci. Res. 85 (12): 2648–56. doi:10.1002/jnr.21176. PMID 17455288.
^ Rosahl TW, Geppert M, Spillane D, Herz J, Hammer RE, Malenka RC, Sudhof TC (1993). "Short-term synaptic plasticity is altered in mice lacking synapsin I". Cell 75 (4): 661–670. doi:10.1016/0092-8674(93)90487-B. PMID 7902212.
^ Kihara AH, Santos TO, Paschon V, Matos RJ, Britto LR (2008). "Lack of photoreceptor signaling alters the expression of specific synaptic proteins in the retina". Neuroscience 151 (4): 995–1005. doi:10.1016/j.neuroscience.2007.09.088. PMID 18248909.
^ Kao HT, Porton B, Hilfiker S, Stefani G, Pieribone VA, DeSalle R, Greengard P (December 1999). "Molecular evolution of the synapsin gene family". J. Exp. Zool. 285 (4): 360–77. doi:10.1002/(SICI)1097-010X(19991215)285:4<360::AID-JEZ4>3.0.CO;2-3. PMID 10578110.
^ Gitler D, Xu Y, Kao HT, Lin D, Lim S, Feng J, Greengard P, Augustine GJ (April 2004). "Molecular determinants of synapsin targeting to presynaptic terminals". J. Neurosci. 24 (14): 3711–20. doi:10.1523/JNEUROSCI.5225-03.2004. PMID 15071120.
^ Ferreira A, Rapoport M (April 2002). "The synapsins: beyond the regulation of neurotransmitter release". Cell. Mol. Life Sci. 59 (4): 589–95. doi:10.1007/s00018-002-8451-5. PMID 12022468.
^ Vawter, MP et al (April 2002). "Reduction of synapsin in the hippocampus of patients with bipolar disorder and schizophrenia". Mol. Psychiatry 7 (6): 571–8. doi:10.1038/sj.mp.4001158. PMID 12140780.

English Journal

Overexpression of tissue-nonspecific alkaline phosphatase increases the expression of neurogenic differentiation markers in the human SH-SY5Y neuroblastoma cell line.

Graser S1, Mentrup B1, Schneider D1, Klein-Hitpass L2, Jakob F1, Hofmann C3.
Bone.Bone.2015 Oct;79:150-61. doi: 10.1016/j.bone.2015.05.033. Epub 2015 May 29.
Patients suffering from the rare hereditary disease hypophosphatasia (HPP), which is based on mutations in the ALPL gene, tend to develop central nervous system (CNS) related issues like epileptic seizures and neuropsychiatric illnesses such as anxiety and depression, in addition to well-known probl
PMID 26032516

Synapsin knockdown is associated with decreased neurite outgrowth, functional synaptogenesis impairment, and fast high-frequency neurotransmitter release.

Brenes O1,2, Giachello CN3, Corradi AM4, Ghirardi M1,5, Montarolo PG1,5.
Journal of neuroscience research.J Neurosci Res.2015 Oct;93(10):1492-506. doi: 10.1002/jnr.23624. Epub 2015 Jul 27.
Synapsins (Syns) are an evolutionarily conserved family of synaptic vesicle-associated proteins related to fine tuning of synaptic transmission. Studies with mammals have partially clarified the different roles of Syns; however, the presence of different genes and isoforms and the development of com
PMID 26213348

Involuntary, forced and voluntary exercises are equally capable of inducing hippocampal plasticity and the recovery of cognitive function after stroke.

Lin Y, Dong J, Yan T, He X, Zheng X, Liang H, Sui M.
Neurological research.Neurol Res.2015 Oct;37(10):893-901. doi: 10.1179/1743132815Y.0000000074. Epub 2015 Jul 16.
OBJECTIVES: Forced and voluntary exercises are known to improve cognition and induce neuroprotection after stroke, however, any effects of involuntary movement induced by functional electrical stimulation (FES) are unclear. The effects of involuntary exercise induced by FES, forced and voluntary exe
PMID 26179091

Japanese Journal

Identification of Pin1-Binding Phosphorylated Proteins in the Mouse Brain

TATARA Yota,TERAKAWA Takahiro,UCHIDA Takafumi
Bioscience, biotechnology, and biochemistry 74(12), 2480-2483, 2010-12-23
… Proteins that involve the neurotransmission pathway, such as synapsin I, synapsin II, and calcium/calmodulin-dependent protein kinase type II (CaMKII), were identified in a Mascot search. …
NAID 10027728301

Identification of an endogenous substrate of zebrafish doublecortin-like protein kinase using a highly active truncation mutant

SHIMOMURA Sachiko,NAGAMINE Tadashi,HATANO Naoya,SUEYOSHI Noriyuki,KAMESHITA Isamu
The journal of biochemistry 147(5), 711-722, 2010-05-01
NAID 10027875877

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Synapsin, ATP binding domain
Identifiers
Symbol	Synapsin_C
Pfam	PF02750
InterPro	IPR001359
PROSITE	PDOC00345
SCOP	1auv
SUPERFAMILY	1auv
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Synapsin, N-terminal domain
	; Structure of the c domain of synapsin IA from bovine brain.
Identifiers
Symbol	Synapsin
Pfam	PF02078
InterPro	IPR001359
PROSITE	PDOC00345
SCOP	1auv
SUPERFAMILY	1auv
OPM superfamily	131
OPM protein	1auv
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

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英: synapsin

-synapsin

[pmid9463376-1] Esser L, Wang CR, Hosaka M, Smagula CS, Südhof TC, Deisenhofer J (February 1998). "Synapsin I is structurally similar to ATP-utilizing enzymes". EMBO J. 17 (4): 977–84. doi:10.1093/emboj/17.4.977. PMC 1170447. PMID 9463376.

[pmid17455288-2] Evergren E, Benfenati F, Shupliakov O (September 2007). "The synapsin cycle: a view from the synaptic endocytic zone". J. Neurosci. Res. 85 (12): 2648–56. doi:10.1002/jnr.21176. PMID 17455288.

[pmid7902212-3] Rosahl TW, Geppert M, Spillane D, Herz J, Hammer RE, Malenka RC, Sudhof TC (1993). "Short-term synaptic plasticity is altered in mice lacking synapsin I". Cell 75 (4): 661–670. doi:10.1016/0092-8674(93)90487-B. PMID 7902212.

[pmid18248909-4] Kihara AH, Santos TO, Paschon V, Matos RJ, Britto LR (2008). "Lack of photoreceptor signaling alters the expression of specific synaptic proteins in the retina". Neuroscience 151 (4): 995–1005. doi:10.1016/j.neuroscience.2007.09.088. PMID 18248909.

[pmid10578110-5] Kao HT, Porton B, Hilfiker S, Stefani G, Pieribone VA, DeSalle R, Greengard P (December 1999). "Molecular evolution of the synapsin gene family". J. Exp. Zool. 285 (4): 360–77. doi:10.1002/(SICI)1097-010X(19991215)285:4<360::AID-JEZ4>3.0.CO;2-3. PMID 10578110.

[pmid15071120-6] Gitler D, Xu Y, Kao HT, Lin D, Lim S, Feng J, Greengard P, Augustine GJ (April 2004). "Molecular determinants of synapsin targeting to presynaptic terminals". J. Neurosci. 24 (14): 3711–20. doi:10.1523/JNEUROSCI.5225-03.2004. PMID 15071120.

[pmid12022468-7] Ferreira A, Rapoport M (April 2002). "The synapsins: beyond the regulation of neurotransmitter release". Cell. Mol. Life Sci. 59 (4): 589–95. doi:10.1007/s00018-002-8451-5. PMID 12022468.

[pmid12140780-8] Vawter, MP et al (April 2002). "Reduction of synapsin in the hippocampus of patients with bipolar disorder and schizophrenia". Mol. Psychiatry 7 (6): 571–8. doi:10.1038/sj.mp.4001158. PMID 12140780.

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synapsin