CPLX1

CPLX1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3RK3, 3RL0
Identifiers
Aliases	CPLX1 , CPX-I, CPX1, complexin 1, EIEE63, DEE63
External IDs	OMIM: 605032 MGI: 104727 HomoloGene: 21324 GeneCards: CPLX1
Gene location (Human)
Chr.	Chromosome 4 (human)
End	826,129 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	108,697,890 bp
RNA expression pattern
	Top expressed in
	external globus pallidus; ; postcentral gyrus; ; pons; ; superior frontal gyrus; ; putamen; ; caudate nucleus; ; Brodmann area 9; ; cerebellar vermis; ; nucleus accumbens; ; cingulate gyrus;
	Top expressed in
	motor neuron; ; substantia nigra; ; facial motor nucleus; ; pontine nuclei; ; lateral geniculate nucleus; ; medial vestibular nucleus; ; habenula; ; anterior horn of spinal cord; ; medial geniculate nucleus; ; dorsal tegmental nucleus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	syntaxin-1 binding ; neurotransmitter transmembrane transporter activity ; syntaxin binding ; SNARE binding ; protein binding ;
Cellular component	cytoplasm ; cytosol ; synapse ; synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex ; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex ; neuronal cell body ; dendrite ; SNARE complex ; protein-containing complex ; presynapse ; calyx of Held ; Schaffer collateral - CA1 synapse ; postsynapse ; glutamatergic synapse ; terminal bouton ;
Biological process	synaptic vesicle exocytosis ; insulin secretion ; regulation of exocytosis ; neurotransmitter transport ; exocytosis ; chemical synaptic transmission ; regulation of synaptic vesicle fusion to presynaptic active zone membrane ; exocytic insertion of neurotransmitter receptor to postsynaptic membrane ; vesicle-mediated transport in synapse ; regulation of neurotransmitter secretion ; neurotransmitter secretion ; glutamate secretion ;
	Sources:Amigo / QuickGO
Orthologs
	10815
	12889
	ENSG00000168993
	ENSMUSG00000033615
	O14810
	P63040
	NM_006651
	NM_007756
	NP_006642
	NP_031782
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 14, 2024

Complexin-1 is a protein that in humans is encoded by the CPLX1 gene.^[5]^[6]

Function

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.^[6]

Interactions

CPLX1 has been shown to interact with SNAP-25 ^[7]^[8] and STX1A.^[9]^[7]^[8]

Related Research Articles

N-ethylmaleimide-sensitive factor, also known as NSF or N-ethylmaleimide sensitive fusion proteins, is an enzyme which in humans is encoded by the NSF gene.

<span class="mw-page-title-main">SNARE protein</span> Protein family

SNARE proteins – "SNAPREceptors" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the release of synaptic vesicles containing neurotransmitters in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

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.

<span class="mw-page-title-main">Synaptotagmin</span>

Synaptotagmins (SYTs) constitute a family of membrane-trafficking proteins that are characterized by an N-terminal transmembrane region (TMR), a variable linker, and two C-terminal C2 domains - C2A and C2B. There are 17 isoforms in the mammalian synaptotagmin family. There are several C2-domain containing protein families that are related to synaptotagmins, including transmembrane (Ferlins, Extended-Synaptotagmin (E-Syt) membrane proteins, and MCTPs) and soluble (RIMS1 and RIMS2, UNC13D, synaptotagmin-related proteins and B/K) proteins. The family includes synaptotagmin 1, a Ca²⁺ sensor in the membrane of the pre-synaptic axon terminal, coded by gene SYT1.

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.

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.

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

Syntaxin-binding protein 1 is a protein that in humans is encoded by the STXBP1 gene. This gene encodes a syntaxin-binding protein. The encoded protein appears to play a role in release of neurotransmitters via regulation of syntaxin, a transmembrane attachment protein receptor. Mutations in this gene have been associated with neurological disorders including epilepsy, intellectual disability, and movement disorders.

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.

Complexin-2 is a protein that in humans is encoded by the CPLX2 gene.

Syntaxin-2, also known as epimorphin, is a protein that in humans is encoded by the STX2 gene.

DnaJ homolog subfamily C member 5, also known as cysteine string protein or CSP is a protein, that in humans encoded by the DNAJC5 gene. It was first described in 1990.

Syntaxin-16 is a protein that in humans is encoded by the STX16 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.

Double C2-like domain-containing protein beta is a protein that in humans is encoded by the DOC2B gene.

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

Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis.

Munc-18 proteins are the mammalian homologue of UNC-18 and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000168993 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033615 - 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, Südhof TC (Oct 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.
1 2 "Entrez Gene: CPLX1 complexin 1".
1 2 Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (Jan 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron. 33 (3): 397–409. doi: 10.1016/S0896-6273(02)00583-4 . PMID 11832227. S2CID 17878965.
1 2 Hu K, Carroll J, Rickman C, Davletov B (Nov 2002). "Action of complexin on SNARE complex". The Journal of Biological Chemistry. 277 (44): 41652–6. doi: 10.1074/jbc.M205044200 . PMID 12200427.
↑ Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Südhof TC, Rizo J (Aug 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal. 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. PMC 1171512 . PMID 10449403.

External links

Human CPLX1 genome location and CPLX1 gene details page in the UCSC Genome Browser .

Abe T (Jun 2002). "[The mechanism of neurotransmitter release: role of synaphin/complexin in synaptic vesicle exocytosis]". Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (7): 794–800. PMID 12058476.
Ishizuka T, Saisu H, Odani S, Abe T (Aug 1995). "Synaphin: a protein associated with the docking/fusion complex in presynaptic terminals". Biochemical and Biophysical Research Communications. 213 (3): 1107–14. doi:10.1006/bbrc.1995.2241. PMID 7654227.
Harrison PJ, Eastwood SL (Nov 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, Kumanishi T, Abe T (Jan 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.
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.
Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (Jan 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron. 33 (3): 397–409. doi: 10.1016/S0896-6273(02)00583-4 . PMID 11832227. S2CID 17878965.
Sawada K, Young CE, Barr AM, Longworth K, Takahashi S, Arango V, Mann JJ, Dwork AJ, Falkai P, Phillips AG, Honer WG (2002). "Altered immunoreactivity of complexin protein in prefrontal cortex in severe mental illness". Molecular Psychiatry. 7 (5): 484–92. doi: 10.1038/sj.mp.4000978 . PMID 12082566.
Basso M, Giraudo S, Corpillo D, Bergamasco B, Lopiano L, Fasano M (Dec 2004). "Proteome analysis of human substantia nigra in Parkinson's disease". Proteomics. 4 (12): 3943–52. doi:10.1002/pmic.200400848. hdl: 11383/1491905 . PMID 15526345. S2CID 23119746.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Giraudo CG, Eng WS, Melia TJ, Rothman JE (Aug 2006). "A clamping mechanism involved in SNARE-dependent exocytosis". Science. 313 (5787): 676–80. Bibcode:2006Sci...313..676G. doi: 10.1126/science.1129450 . PMID 16794037. S2CID 28309295.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000168993 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033615 - 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, Südhof TC (Oct 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.

[entrez-6] 1 2 "Entrez Gene: CPLX1 complexin 1".

[pmid11832227-7] 1 2 Chen X, Tomchick DR, Kovrigin E, Araç D, Machius M, Südhof TC, Rizo J (Jan 2002). "Three-dimensional structure of the complexin/SNARE complex". Neuron. 33 (3): 397–409. doi: 10.1016/S0896-6273(02)00583-4 . PMID 11832227. S2CID 17878965.

[pmid12200427-8] 1 2 Hu K, Carroll J, Rickman C, Davletov B (Nov 2002). "Action of complexin on SNARE complex". The Journal of Biological Chemistry. 277 (44): 41652–6. doi: 10.1074/jbc.M205044200 . PMID 12200427.

[pmid10449403-9] Dulubova I, Sugita S, Hill S, Hosaka M, Fernandez I, Südhof TC, Rizo J (Aug 1999). "A conformational switch in syntaxin during exocytosis: role of munc18". The EMBO Journal. 18 (16): 4372–82. doi:10.1093/emboj/18.16.4372. PMC 1171512 . PMID 10449403.

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