CPLX2

CPLX2
Identifiers
Aliases	CPLX2 , 921-L, CPX-2, CPX2, Hfb1, complexin 2
External IDs	OMIM: 605033 MGI: 104726 HomoloGene: 38212 GeneCards: CPLX2
Gene location (Human)
Chr.	Chromosome 5 (human)
End	175,884,021 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	54,531,730 bp
RNA expression pattern
	Top expressed in
	amygdala; ; caudate nucleus; ; dorsolateral prefrontal cortex; ; prefrontal cortex; ; nucleus accumbens; ; hippocampus proper; ; postcentral gyrus; ; putamen; ; entorhinal cortex; ; Brodmann area 9;
	Top expressed in
	superior frontal gyrus; ; olfactory tubercle; ; cerebellar cortex; ; nucleus accumbens; ; globus pallidus; ; subiculum; ; cerebellar vermis; ; piriform cortex; ; superior colliculus; ; primary motor cortex;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	syntaxin-1 binding ; syntaxin binding ; SNARE binding ; calcium-dependent protein binding ;
Cellular component	cytoplasm ; cytosol ; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex ; mast cell granule ; synapse ; synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex ; neuronal cell body ; dendrite ; SNARE complex ; presynapse ; calyx of Held ; postsynapse ; glutamatergic synapse ; terminal bouton ;
Biological process	cell differentiation ; synaptic vesicle exocytosis ; nervous system development ; positive regulation of synaptic plasticity ; vesicle docking involved in exocytosis ; regulation of exocytosis ; mast cell degranulation ; neurotransmitter transport ; exocytosis ; regulation of synaptic vesicle fusion to presynaptic active zone membrane ; regulation of neurotransmitter secretion ;
	Sources:Amigo / QuickGO
Orthologs
	10814
	12890
	ENSG00000145920
	ENSMUSG00000025867
	Q6PUV4
	P84086
	NM_001008220 ; NM_006650 ; NM_032282
	NM_009946 ; NM_001362218
	NP_001008221 ; NP_006641
	NP_034076 ; NP_001349147
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 14, 2024

Complexin-2 is a protein that in humans is encoded by the CPLX2 gene.^[5]^[6]^[7]

Proteins encoded by the complexin/synaphin gene family are cytosolic proteins that function in synaptic vesicle exocytosis. These proteins bind syntaxin, part of the SNAP receptor. The protein product of this gene binds to the SNAP receptor complex and disrupts it, allowing transmitter release. Two transcript variants encoding the same protein have been found for this gene.^[7]

Related Research Articles

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. 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.

Complexin (also known as synaphin) refers to a one of a small set of eukaryotic cytoplasmic neuronal proteins which binds to the SNARE protein complex (SNAREpin) with a high affinity. These are called synaphin 1 and 2. In the presence of Ca²⁺, the transport vesicle protein synaptotagmin displaces complexin, allowing the SNARE protein complex to bind the transport vesicle to the presynaptic membrane.

Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.

Disks large homolog 3 (DLG3) also known as neuroendocrine-DLG or synapse-associated protein 102 (SAP-102) is a protein that in humans is encoded by the DLG3 gene. DLG3 is a member of the membrane-associated guanylate kinase (MAGUK) superfamily of proteins.

Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.

Glutamate receptor 1 is a protein that in humans is encoded by the GRIA1 gene.

Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene.

N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.

Regulating synaptic membrane exocytosis protein 1 is a protein that in humans is encoded by the RIMS1 gene.

Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.

Rabphilin-3A is a protein that in humans is encoded by the RPH3A gene. It contains two C2 domains and binds calcium ions at low micromolar concentration. Rabphilin was shown to regulate neurotransmitter release in hippocampal neurons after neurons had an increased synaptic activity and their release rate was depressed.

Syntaxin-binding protein 2 is a protein that in humans is encoded by the STXBP2 gene.

Neurabin-2 is a protein that in humans is encoded by the PPP1R9B gene.

Regulating synaptic membrane exocytosis protein 2 is a protein that in humans is encoded by the RIMS2 gene.

Complexin-1 is a protein that in humans is encoded by the CPLX1 gene.

Potassium voltage-gated channel subfamily KQT member 5 is a protein that in humans is encoded by the KCNQ5 gene.

Glutamate receptor, ionotropic kainate 5 is a protein that in humans is encoded by the GRIK5 gene.

Syntaxin-binding protein 5 is a protein that in humans is encoded by the STXBP5 gene. It is also known as tomosyn, after 友, "friend" in Japanese, for its role as a binding protein.

Ryanodine receptor 3 is one of a class of ryanodine receptors and a protein that in humans is encoded by the RYR3 gene. The protein encoded by this gene is both a calcium channel and a receptor for the plant alkaloid ryanodine. RYR3 and RYR1 control the resting calcium ion concentration in skeletal muscle.

Syntaxin 3, also known as STX3, is a protein which in humans is encoded by the STX3 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000145920 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025867 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ McMahon HT, Missler M, Li C, Sudhof TC (Nov 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi: 10.1016/0092-8674(95)90239-2 . PMID 7553862. S2CID 675343.
↑ Raevskaya NM, Dergunova LV, Vladychenskaya IP, Stavchansky VV, Oborina MV, Poltaraus AB, Limborska SA (Sep 2005). "Structural organization of the human complexin 2 gene (CPLX2) and aspects of its functional activity". Gene. 359: 127–37. doi:10.1016/j.gene.2005.07.005. PMID 16162394.
1 2 "Entrez Gene: CPLX2 complexin 2".

External links

Human CPLX2 genome location and CPLX2 gene details page in the UCSC Genome Browser .

Abe T (2002). "[The mechanism of neurotransmitter release: role of synaphin/complexin in synaptic vesicle exocytosis]". Tanpakushitsu Kakusan Koso. 47 (7): 794–800. PMID 12058476.
Christensen VL, Johnston NP (1978). "Effect of time of day of insemination and the position of the egg in the oviduct on the fertility of turkeys". Poult. Sci. 56 (2): 458–62. doi: 10.3382/ps.0560458 . PMID 605033.
Morgans CW, Brandstätter JH, Kellerman J, et al. (1996). "A SNARE complex containing syntaxin 3 is present in ribbon synapses of the retina". J. Neurosci. 16 (21): 6713–21. doi: 10.1523/JNEUROSCI.16-21-06713.1996 . PMC 6579260 . PMID 8824312.
Harrison PJ, Eastwood SL (1998). "Preferential involvement of excitatory neurons in medial temporal lobe in schizophrenia". Lancet. 352 (9141): 1669–73. doi:10.1016/S0140-6736(98)03341-8. PMID 9853440. S2CID 45239545.
Ishizuka T, Saisu H, Odani S, et al. (1999). "Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex". Neuroscience. 88 (1): 295–306. doi:10.1016/S0306-4522(98)00223-1. PMID 10051208. S2CID 46636775.
Yamada M, Saisu H, Ishizuka T, et al. (1999). "Immunohistochemical distribution of the two isoforms of synaphin/complexin involved in neurotransmitter release: localization at the distinct central nervous system regions and synaptic types". Neuroscience. 93 (1): 7–18. doi:10.1016/S0306-4522(99)00104-9. PMID 10430466. S2CID 21532356.
Pabst S, Hazzard JW, Antonin W, et al. (2000). "Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions". J. Biol. Chem. 275 (26): 19808–18. doi: 10.1074/jbc.M002571200 . PMID 10777504.
Eastwood SL, Cotter D, Harrison PJ (2001). "Cerebellar synaptic protein expression in schizophrenia". Neuroscience. 105 (1): 219–29. doi:10.1016/S0306-4522(01)00141-5. PMID 11483314. S2CID 34257327.
Eastwood SL, Harrison PJ (2001). "Synaptic pathology in the anterior cingulate cortex in schizophrenia and mood disorders. A review and a Western blot study of synaptophysin, GAP-43 and the complexins". Brain Res. Bull. 55 (5): 569–78. doi:10.1016/S0361-9230(01)00530-5. PMID 11576753. S2CID 23012653.
Pabst S, Margittai M, Vainius D, et al. (2002). "Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis". J. Biol. Chem. 277 (10): 7838–48. doi: 10.1074/jbc.M109507200 . hdl: 11858/00-001M-0000-0012-F415-9 . PMID 11751907.
Sawada K, Young CE, Barr AM, et al. (2002). "Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness". Mol. Psychiatry. 7 (5): 484–92. doi: 10.1038/sj.mp.4000978 . PMID 12082566.
Hu K, Carroll J, Rickman C, Davletov B (2003). "Action of complexin on SNARE complex". J. Biol. Chem. 277 (44): 41652–6. doi: 10.1074/jbc.M205044200 . PMID 12200427.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Edwardson JM, Wang CT, Gong B, et al. (2003). "Expression of mutant huntingtin blocks exocytosis in PC12 cells by depletion of complexin II". J. Biol. Chem. 278 (33): 30849–53. doi: 10.1074/jbc.M304615200 . PMID 12807877.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Eastwood SL, Harrison PJ (2005). "Decreased expression of vesicular glutamate transporter 1 and complexin II mRNAs in schizophrenia: further evidence for a synaptic pathology affecting glutamate neurons". Schizophr. Res. 73 (2–3): 159–72. doi:10.1016/j.schres.2004.05.010. PMID 15653259. S2CID 2335413.
DiProspero NA, Chen EY, Charles V, et al. (2005). "Early changes in Huntington's disease patient brains involve alterations in cytoskeletal and synaptic elements". J. Neurocytol. 33 (5): 517–33. doi:10.1007/s11068-004-0514-8. PMID 15906159. S2CID 20082165.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000145920 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025867 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7553862-5] McMahon HT, Missler M, Li C, Sudhof TC (Nov 1995). "Complexins: cytosolic proteins that regulate SNAP receptor function". Cell. 83 (1): 111–9. doi: 10.1016/0092-8674(95)90239-2 . PMID 7553862. S2CID 675343.

[pmid16162394-6] Raevskaya NM, Dergunova LV, Vladychenskaya IP, Stavchansky VV, Oborina MV, Poltaraus AB, Limborska SA (Sep 2005). "Structural organization of the human complexin 2 gene (CPLX2) and aspects of its functional activity". Gene. 359: 127–37. doi:10.1016/j.gene.2005.07.005. PMID 16162394.

[entrez-7] 1 2 "Entrez Gene: CPLX2 complexin 2".

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CPLX2

Contents

Related Research Articles

References

External links

Further reading