CASPR also known as Contactin associated protein 1, Paranodin and CASPR1 is a protein that in humans is encoded by the CNTNAP1 gene.[5] CASPR is a part of the neurexin family of proteins, hence its another name "Neurexin IV".[6] CASPR is a membrane protein found in the neuronal membrane in the paranodal section of the axon[[]] in myelinated neurons, between the Nodes of Ranvier containing Na+ channels, and juxtaparanode, which contains K+ channels.[7] During myelination, caspr associates with contactin in a cis complex,[7] though its precise role in myelination is not yet understood.
The gene product was initially identified as a 190-kD protein associated with the contactin-PTPRZ1 complex. The 1,384-amino acid protein, also designated p190 or CASPR for 'contactin-associated protein,' includes an extracellular domain with several putative protein-protein interaction domains, a putative transmembrane domain, and a 74-amino acid cytoplasmic domain. Northern blot analysis showed that the gene is transcribed predominantly in brain as a transcript of 6.2 kb, with weak expression in several other tissues tested. The architecture of its extracellular domain is similar to that of neurexins, and this protein may be the signaling subunit of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons. [provided by RefSeq, Jan 2009].
^ abRios JC, Melendez-Vasquez CV, Einheber S, Lustig M, Grumet M, Hemperly J, et al. (15 November 2000). "Contactin-Associated Protein (Caspr) and Contactin Form a Complex That Is Targeted to the Paranodal Junctions during Myelination". J. Neurosci. 20 (22): 8354–8364. doi:10.1523/JNEUROSCI.20-22-08354.2000. PMC6773165. PMID 11069942.
^Laquérriere A, Maluenda J, Camus A, Fontenas L, Dieterich K, Nolent F, et al. (May 2014). "Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis multiplex congenita with axoglial defects". Human Molecular Genetics. 23 (9): 2279–89. doi:10.1093/hmg/ddt618. PMID 24319099.
^Sabbagh S, Antoun S, Mégarbané A (2020) CNTNAP1 Mutations and Their Clinical Presentations: New Case Report and Systematic Review. Case Rep Med 2020:8795607.
Further readingedit
Martins-de-Souza D, Guest PC, Mann DM, Roeber S, Rahmoune H, Bauder C, et al. (April 2012). "Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration". Journal of Proteome Research. 11 (4): 2533–43. doi:10.1021/pr2012279. PMID 22360420.
Velez Edwards DR, Naj AC, Monda K, North KE, Neuhouser M, Magvanjav O, et al. (March 2013). "Gene-environment interactions and obesity traits among postmenopausal African-American and Hispanic women in the Women's Health Initiative SHARe Study". Human Genetics. 132 (3): 323–36. doi:10.1007/s00439-012-1246-3. PMC3704217. PMID 23192594.
Li R, Zhang B, Zheng Y (December 1997). "Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190". The Journal of Biological Chemistry. 272 (52): 32830–5. doi:10.1074/jbc.272.52.32830. PMID 9407060.
Lee JY, Park AK, Lee KM, Park SK, Han S, Han W, et al. (September 2009). "Candidate gene approach evaluates association between innate immunity genes and breast cancer risk in Korean women". Carcinogenesis. 30 (9): 1528–31. doi:10.1093/carcin/bgp084. PMID 19372141.
Peles E, Nativ M, Lustig M, Grumet M, Schilling J, Martinez R, et al. (March 1997). "Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions". The EMBO Journal. 16 (5): 978–88. doi:10.1093/emboj/16.5.978. PMC1169698. PMID 9118959.
Hur JY, Teranishi Y, Kihara T, Yamamoto NG, Inoue M, Hosia W, et al. (April 2012). "Identification of novel γ-secretase-associated proteins in detergent-resistant membranes from brain". The Journal of Biological Chemistry. 287 (15): 11991–2005. doi:10.1074/jbc.M111.246074. PMC3320946. PMID 22315232.
Venken K, Meuleman J, Irobi J, Ceuterick C, Martini R, De Jonghe P, et al. (August 2001). "Caspr1/Paranodin/Neurexin IV is most likely not a common disease-causing gene for inherited peripheral neuropathies". NeuroReport. 12 (11): 2609–14. doi:10.1097/00001756-200108080-00063. PMID 11496158. S2CID 28331998.
Charles P, Tait S, Faivre-Sarrailh C, Barbin G, Gunn-Moore F, Denisenko-Nehrbass N, et al. (February 2002). "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Current Biology. 12 (3): 217–20. Bibcode:2002CBio...12..217C. doi:10.1016/S0960-9822(01)00680-7. PMID 11839274. S2CID 18017227.
Nie DY, Zhou ZH, Ang BT, Teng FY, Xu G, Xiang T, et al. (November 2003). "Nogo-A at CNS paranodes is a ligand of Caspr: possible regulation of K(+) channel localization". The EMBO Journal. 22 (21): 5666–78. doi:10.1093/emboj/cdg570. PMC275427. PMID 14592966.
External linksedit
Human CNTNAP1 genome location and CNTNAP1 gene details page in the UCSC Genome Browser.
caspr, confused, with, crispr, also, known, contactin, associated, protein, paranodin, protein, that, humans, encoded, cntnap1, gene, part, neurexin, family, proteins, hence, another, name, neurexin, membrane, protein, found, neuronal, membrane, paranodal, sec. Not to be confused with CRISPR CASPR also known as Contactin associated protein 1 Paranodin and CASPR1 is a protein that in humans is encoded by the CNTNAP1 gene 5 CASPR is a part of the neurexin family of proteins hence its another name Neurexin IV 6 CASPR is a membrane protein found in the neuronal membrane in the paranodal section of the axon in myelinated neurons between the Nodes of Ranvier containing Na channels and juxtaparanode which contains K channels 7 During myelination caspr associates with contactin in a cis complex 7 though its precise role in myelination is not yet understood CNTNAP1IdentifiersAliasesCNTNAP1 CASPR CNTNAP NRXN4 P190 contactin associated protein 1 CHN3External IDsOMIM 602346 MGI 1858201 HomoloGene 2693 GeneCards CNTNAP1Gene location Human Chr Chromosome 17 human 1 Band17q21 2Start42 682 531 bp 1 End42 699 993 bp 1 Gene location Mouse Chr Chromosome 11 mouse 2 Band11 11 DStart101 061 349 bp 2 End101 081 550 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inRegion I of hippocampus properpostcentral gyrusBrodmann area 46superior frontal gyrusorbitofrontal cortexprefrontal cortexBrodmann area 9entorhinal cortexcingulate gyruscerebellar vermisTop expressed insuperior frontal gyruscerebellar cortexsecondary oocyteentorhinal cortexliphippocampus properinferior colliculusmedulla oblongatasuperior colliculusdorsomedial hypothalamic nucleusMore reference expression dataBioGPSn aGene ontologyMolecular functionSH3 domain binding protein binding signaling receptor activityCellular componentintegral component of membrane membrane myelin sheath voltage gated potassium channel complex integral component of plasma membrane axon paranode region of axon cell junction paranodal junction presynaptic active zone membraneBiological processneuromuscular process controlling posture neuromuscular process controlling balance protein localization to paranode region of axon cell adhesion cytoskeleton organization neuronal action potential propagation neuron projection development signal transduction positive regulation of signal transduction central nervous system myelination myelination in peripheral nervous system paranodal junction assembly neuron projection morphogenesis protein localization to juxtaparanode region of axonSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez850653321EnsemblENSG00000108797ENSMUSG00000017167UniProtP78357O54991RefSeq mRNA NM 003632NM 016782RefSeq protein NP 003623NP 058062Location UCSC Chr 17 42 68 42 7 MbChr 11 101 06 101 08 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Clinical 3 References 4 Further reading 5 External linksFunction editThe gene product was initially identified as a 190 kD protein associated with the contactin PTPRZ1 complex The 1 384 amino acid protein also designated p190 or CASPR for contactin associated protein includes an extracellular domain with several putative protein protein interaction domains a putative transmembrane domain and a 74 amino acid cytoplasmic domain Northern blot analysis showed that the gene is transcribed predominantly in brain as a transcript of 6 2 kb with weak expression in several other tissues tested The architecture of its extracellular domain is similar to that of neurexins and this protein may be the signaling subunit of contactin enabling recruitment and activation of intracellular signaling pathways in neurons provided by RefSeq Jan 2009 Clinical editMutations in CNTNAP1 cause arthrogryposis multiplex congenita 8 Other diseases associated with mutations in this gene include lethal congenital contracture syndrome type 7 and congenital hypomyelinating neuropathy type 3 9 References edit a b c GRCh38 Ensembl release 89 ENSG00000108797 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000017167 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 Entrez Gene Contactin associated protein 1 OMIM Entry 602346 CONTACTIN ASSOCIATED PROTEIN 1 CNTNAP1 omim org Retrieved 2017 04 27 a b Rios JC Melendez Vasquez CV Einheber S Lustig M Grumet M Hemperly J et al 15 November 2000 Contactin Associated Protein Caspr and Contactin Form a Complex That Is Targeted to the Paranodal Junctions during Myelination J Neurosci 20 22 8354 8364 doi 10 1523 JNEUROSCI 20 22 08354 2000 PMC 6773165 PMID 11069942 Laquerriere A Maluenda J Camus A Fontenas L Dieterich K Nolent F et al May 2014 Mutations in CNTNAP1 and ADCY6 are responsible for severe arthrogryposis multiplex congenita with axoglial defects Human Molecular Genetics 23 9 2279 89 doi 10 1093 hmg ddt618 PMID 24319099 Sabbagh S Antoun S Megarbane A 2020 CNTNAP1 Mutations and Their Clinical Presentations New Case Report and Systematic Review Case Rep Med 2020 8795607 Further reading editMartins de Souza D Guest PC Mann DM Roeber S Rahmoune H Bauder C et al April 2012 Proteomic analysis identifies dysfunction in cellular transport energy and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration Journal of Proteome Research 11 4 2533 43 doi 10 1021 pr2012279 PMID 22360420 Velez Edwards DR Naj AC Monda K North KE Neuhouser M Magvanjav O et al March 2013 Gene environment interactions and obesity traits among postmenopausal African American and Hispanic women in the Women s Health Initiative SHARe Study Human Genetics 132 3 323 36 doi 10 1007 s00439 012 1246 3 PMC 3704217 PMID 23192594 Li R Zhang B Zheng Y December 1997 Structural determinants required for the interaction between Rho GTPase and the GTPase activating domain of p190 The Journal of Biological Chemistry 272 52 32830 5 doi 10 1074 jbc 272 52 32830 PMID 9407060 Lee JY Park AK Lee KM Park SK Han S Han W et al September 2009 Candidate gene approach evaluates association between innate immunity genes and breast cancer risk in Korean women Carcinogenesis 30 9 1528 31 doi 10 1093 carcin bgp084 PMID 19372141 Peles E Nativ M Lustig M Grumet M Schilling J Martinez R et al March 1997 Identification of a novel contactin associated transmembrane receptor with multiple domains implicated in protein protein interactions The EMBO Journal 16 5 978 88 doi 10 1093 emboj 16 5 978 PMC 1169698 PMID 9118959 Hur JY Teranishi Y Kihara T Yamamoto NG Inoue M Hosia W et al April 2012 Identification of novel g secretase associated proteins in detergent resistant membranes from brain The Journal of Biological Chemistry 287 15 11991 2005 doi 10 1074 jbc M111 246074 PMC 3320946 PMID 22315232 Venken K Meuleman J Irobi J Ceuterick C Martini R De Jonghe P et al August 2001 Caspr1 Paranodin Neurexin IV is most likely not a common disease causing gene for inherited peripheral neuropathies NeuroReport 12 11 2609 14 doi 10 1097 00001756 200108080 00063 PMID 11496158 S2CID 28331998 Charles P Tait S Faivre Sarrailh C Barbin G Gunn Moore F Denisenko Nehrbass N et al February 2002 Neurofascin is a glial receptor for the paranodin Caspr contactin axonal complex at the axoglial junction Current Biology 12 3 217 20 Bibcode 2002CBio 12 217C doi 10 1016 S0960 9822 01 00680 7 PMID 11839274 S2CID 18017227 Nie DY Zhou ZH Ang BT Teng FY Xu G Xiang T et al November 2003 Nogo A at CNS paranodes is a ligand of Caspr possible regulation of K channel localization The EMBO Journal 22 21 5666 78 doi 10 1093 emboj cdg570 PMC 275427 PMID 14592966 External links editHuman CNTNAP1 genome location and CNTNAP1 gene details page in the UCSC Genome Browser This article incorporates text from the United States National Library of Medicine which is in the public domain nbsp This article on a gene on human chromosome 17 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title CASPR amp oldid 1215110969, wikipedia, wiki, book, books, library,
