Biology:NFASC
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Neurofascin is a protein that in humans is encoded by the NFASC gene.[1][2][3]
Function
Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM) involved in axon subcellular targeting and synapse formation during neural development.[3][4]
Clinical importance
A homozygous mutation causing loss of Nfasc155 causes severe congenital hypotonia, contractures of fingers and toes and no reaction to touch or pain.[5]
References
- ↑ "Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily". The Journal of Cell Biology 118 (1): 149–61. July 1992. doi:10.1083/jcb.118.1.149. PMID 1377696.
- ↑ "Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes". Mammalian Genome 7 (7): 558–9. July 1996. doi:10.1007/s003359900168. PMID 8672144.
- ↑ 3.0 3.1 "Entrez Gene: NFASC neurofascin homolog (chicken)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23114.
- ↑ "Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment". Cell 119 (2): 257–72. October 2004. doi:10.1016/j.cell.2004.10.004. PMID 15479642.
- ↑ "Homozygous mutation in the Neurofascin gene affecting the glial isoform of Neurofascin causes severe neurodevelopment disorder with hypotonia, amimia and areflexia". Human Molecular Genetics 27 (21): 3669–3674. August 2018. doi:10.1093/hmg/ddy277. PMID 30124836.
Further reading
- "The L1 family of neural cell adhesion molecules: old proteins performing new tricks". Neuron 17 (4): 587–93. October 1996. doi:10.1016/S0896-6273(00)80192-0. PMID 8893017.
- "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research 9 (3): 99–106. June 2002. doi:10.1093/dnares/9.3.99. PMID 12168954.
- "The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation". Proceedings of the National Academy of Sciences of the United States of America 94 (24): 12957–62. November 1997. doi:10.1073/pnas.94.24.12957. PMID 9371782. Bibcode: 1997PNAS...9412957T.
- "Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules". Journal of Neurochemistry 70 (5): 1839–49. May 1998. doi:10.1046/j.1471-4159.1998.70051839.x. PMID 9572267.
- "Structural requirements for association of neurofascin with ankyrin". The Journal of Biological Chemistry 273 (46): 30785–94. November 1998. doi:10.1074/jbc.273.46.30785. PMID 9804856.
- "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research 5 (5): 277–86. October 1998. doi:10.1093/dnares/5.5.277. PMID 9872452.
- "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity". The Journal of Biological Chemistry 276 (14): 10646–54. April 2001. doi:10.1074/jbc.M010647200. PMID 11152476.
- "Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain". The Journal of Cell Biology 154 (2): 427–34. July 2001. doi:10.1083/jcb.200102086. PMID 11470829.
- "FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons". Journal of Cell Science 114 (Pt 21): 3823–35. November 2001. doi:10.1242/jcs.114.21.3823. PMID 11719549. https://cdr.lib.unc.edu/downloads/k930c607k.
- "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments". The Journal of Cell Biology 155 (5): 739–46. November 2001. doi:10.1083/jcb.200109026. PMID 11724816.
- "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Current Biology 12 (3): 217–20. February 2002. doi:10.1016/S0960-9822(01)00680-7. PMID 11839274.
- "A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin". The Journal of Neuroscience 22 (18): 7948–58. September 2002. doi:10.1523/jneurosci.22-18-07948.2002. PMID 12223548.
- "Caspr regulates the processing of contactin and inhibits its binding to neurofascin". The Journal of Cell Biology 163 (6): 1213–8. December 2003. doi:10.1083/jcb.200309147. PMID 14676309.
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