NFASC

From Wikipedia, the free encyclopedia

Neurofascin homolog (chicken)

Identifiers

NFASC; DKFZp686P2250; FLJ46866; KIAA0756; NF; NRCAML

External IDs

OMIM: 609145 MGI: 104753 HomoloGene: 24945

Gene ontology
Molecular Function:	• protein binding
Cellular Component:	• plasma membrane • integral to membrane • axon
Biological Process:	• cell adhesion • axon guidance • synapse organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015090 (mRNA)
NP_055905 (protein)

NM_182716 (mRNA)
NP_874385 (protein)

Location

Chr 1: 203.06 - 203.26 Mb

Chr 1: 134.4 - 134.53 Mb

Pubmed search

[1]

[2]

Neurofascin homolog (chicken), also known as NFASC, is a human gene.^[1]

Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM; MIM 308840) involved in axon subcellular targeting and synapse formation during neural development (Ango et al., 2004).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: NFASC neurofascin homolog (chicken).

[edit] Further reading

Hortsch M (1996). "The L1 family of neural cell adhesion molecules: old proteins performing new tricks.". Neuron 17 (4): 587–93. PMID 8893017.
Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Volkmer H, Hassel B, Wolff JM, et al. (1992). "Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily.". J. Cell Biol. 118 (1): 149–61. PMID 1377696.
Burmeister M, Ren Q, Makris GJ, et al. (1996). "Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes.". Mamm. Genome 7 (7): 558–9. PMID 8672144.
Tuvia S, Garver TD, Bennett V (1998). "The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation.". Proc. Natl. Acad. Sci. U.S.A. 94 (24): 12957–62. PMID 9371782.
Ren Q, Bennett V (1998). "Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules.". J. Neurochem. 70 (5): 1839–49. PMID 9572267.
Zhang X, Davis JQ, Carpenter S, Bennett V (1998). "Structural requirements for association of neurofascin with ankyrin.". J. Biol. Chem. 273 (46): 30785–94. PMID 9804856.
Nagase T, Ishikawa K, Suyama M, et al. (1999). "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 Res. 5 (5): 277–86. PMID 9872452.
Koroll M, Rathjen FG, Volkmer H (2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity.". J. Biol. Chem. 276 (14): 10646–54. doi:10.1074/jbc.M010647200. PMID 11152476.
Ratcliffe CF, Westenbroek RE, Curtis R, Catterall WA (2001). "Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain.". J. Cell Biol. 154 (2): 427–34. PMID 11470829.
Jenkins SM, Kizhatil K, Kramarcy NR, et al. (2002). "FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons.". J. Cell. Sci. 114 (Pt 21): 3823–35. PMID 11719549.
Jenkins SM, Bennett V (2002). "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments.". J. Cell Biol. 155 (5): 739–46. doi:10.1083/jcb.200109026. PMID 11724816.
Charles P, Tait S, Faivre-Sarrailh C, et al. (2002). "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction.". Curr. Biol. 12 (3): 217–20. PMID 11839274.
Kizhatil K, Wu YX, Sen A, Bennett V (2002). "A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.". J. Neurosci. 22 (18): 7948–58. PMID 12223548.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Gollan L, Salomon D, Salzer JL, Peles E (2004). "Caspr regulates the processing of contactin and inhibits its binding to neurofascin.". J. Cell Biol. 163 (6): 1213–8. doi:10.1083/jcb.200309147. PMID 14676309.
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.
Ango F, di Cristo G, Higashiyama H, et al. (2004). "Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment.". Cell 119 (2): 257–72. doi:10.1016/j.cell.2004.10.004. PMID 15479642.