Biology:Contactin 1
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Contactin 1, also known as CNTN1, is a protein which in humans is encoded by the CNTN1 gene.[1][2]
Function
The protein encoded by this gene is a member of the immunoglobulin superfamily. It is a glycosylphosphatidylinositol (GPI)-anchored neuronal membrane protein that functions as a cell adhesion molecule. It may play a role in the formation of axon connections in the developing nervous system. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[2]
Interactions
CNTN1 has been shown to interact with PTPRB.[3][4]
References
- ↑ "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12". Genomics 21 (3): 571–82. Jun 1994. doi:10.1006/geno.1994.1316. PMID 7959734.
- ↑ 2.0 2.1 "Entrez Gene: CNTN1 contactin 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1272.
- ↑ "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". The Journal of Cell Biology 136 (4): 907–18. Feb 1997. doi:10.1083/jcb.136.4.907. PMID 9049255.
- ↑ "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell 82 (2): 251–60. Jul 1995. doi:10.1016/0092-8674(95)90312-7. PMID 7628014.
External links
- Human CNTN1 genome location and CNTN1 gene details page in the UCSC Genome Browser.
- Human F3 genome location and F3 gene details page in the UCSC Genome Browser.
Further reading
- "Glycosylphosphatidylinositol anchored recognition molecules that function in axonal fasciculation, growth and guidance in the nervous system". Cell Biology International Reports 15 (11): 1151–66. Nov 1991. doi:10.1016/0309-1651(91)90061-M. PMID 1838307.
- "Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling". Trends in Biochemical Sciences 23 (4): 121–4. Apr 1998. doi:10.1016/S0968-0004(98)01195-5. PMID 9584610.
- "The F3 neuronal glycosylphosphatidylinositol-linked molecule is localized to glycolipid-enriched membrane subdomains and interacts with L1 and fyn kinase in cerebellum". Journal of Neurochemistry 65 (5): 2307–17. Nov 1995. doi:10.1046/j.1471-4159.1995.65052307.x. PMID 7595520.
- "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell 82 (2): 251–60. Jul 1995. doi:10.1016/0092-8674(95)90312-7. PMID 7628014.
- "Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12". Genomics 21 (3): 571–82. Jun 1994. doi:10.1006/geno.1994.1316. PMID 7959734.
- "Identification and characterization of the human cell adhesion molecule contactin". Brain Research. Molecular Brain Research 21 (1–2): 1–8. Jan 1994. doi:10.1016/0169-328X(94)90372-7. PMID 8164510.
- "Overlapping and differential expression of BIG-2, BIG-1, TAG-1, and F3: four members of an axon-associated cell adhesion molecule subgroup of the immunoglobulin superfamily". Journal of Neurobiology 28 (1): 51–69. Sep 1995. doi:10.1002/neu.480280106. PMID 8586965.
- "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". The Journal of Cell Biology 136 (4): 907–18. Feb 1997. doi:10.1083/jcb.136.4.907. PMID 9049255.
- "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11". The European Journal of Neuroscience 8 (4): 766–82. Apr 1996. doi:10.1111/j.1460-9568.1996.tb01262.x. PMID 9081628.
- "Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R". Journal of Neuroscience Research 49 (6): 698–709. Sep 1997. doi:10.1002/(SICI)1097-4547(19970915)49:6<698::AID-JNR4>3.0.CO;2-2. PMID 9335257.
- "Regulated expression of the cell adhesion glycoprotein F3 in adult hypothalamic magnocellular neurons". The Journal of Neuroscience 18 (14): 5333–43. Jul 1998. doi:10.1523/JNEUROSCI.18-14-05333.1998. PMID 9651216.
- "The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling between neurons and glial cells". The European Journal of Neuroscience 11 (4): 1134–47. Apr 1999. doi:10.1046/j.1460-9568.1999.00521.x. PMID 10103110.
- "Ataxia and abnormal cerebellar microorganization in mice with ablated contactin gene expression". Neuron 24 (3): 739–50. Nov 1999. doi:10.1016/S0896-6273(00)81126-5. PMID 10595523.
- "Mobilization of the cell adhesion glycoprotein F3/contactin to axonal surfaces is activity dependent". The European Journal of Neuroscience 14 (4): 645–56. Aug 2001. doi:10.1046/j.0953-816x.2001.01682.x. PMID 11556889.
- "Contactin associates with Na+ channels and increases their functional expression". The Journal of Neuroscience 21 (19): 7517–25. Oct 2001. doi:10.1523/JNEUROSCI.21-19-07517.2001. PMID 11567041.
- "Analysis of interactions of the adhesion molecule TAG-1 and its domains with other immunoglobulin superfamily members". Molecular and Cellular Neurosciences 20 (3): 367–81. Jul 2002. doi:10.1006/mcne.2002.1105. PMID 12139915.
- "Phosphacan short isoform, a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-beta, interacts with neuronal receptors and promotes neurite outgrowth". The Journal of Biological Chemistry 278 (26): 24164–73. Jun 2003. doi:10.1074/jbc.M211721200. PMID 12700241.
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