Biology:FNBP1L
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 Generic protein structure example |
Formin-binding protein 1-like is a protein that in humans is encoded by the FNBP1L gene.[1][2]
Function
The protein encoded by this gene binds to both CDC42 and N-WASP. This protein promotes CDC42-induced actin polymerization by activating the N-WASP-WIP complex and, therefore, is involved in a pathway that links cell surface signals to the actin cytoskeleton. Alternative splicing results in multiple transcript variants encoding different isoforms.[2]
Clinical significance
FNBP1L polymorphisms, specifically the SNP rs236330 has been associated with normally varying intelligence differences in adults[3] and in children.[4]
References
- ↑ "Identification and characterization of human FNBP1L gene in silico". Int J Mol Med 13 (1): 157–62. Dec 2003. doi:10.3892/ijmm.13.1.157. PMID 14654988.
- ↑ 2.0 2.1 "Entrez Gene: FNBP1L formin binding protein 1-like". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54874.
- ↑ "Genome-wide association studies establish that human intelligence is highly heritable and polygenic". Mol. Psychiatry 16 (10): 996–1005. October 2011. doi:10.1038/mp.2011.85. PMID 21826061.
- ↑ "Childhood intelligence is heritable, highly polygenic and associated with FNBP1L". Mol. Psychiatry 19 (2): 253–8. January 2013. doi:10.1038/mp.2012.184. PMID 23358156.
Further reading
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932.
- "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039.
- "Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex". Cell 118 (2): 203–16. 2004. doi:10.1016/j.cell.2004.06.027. PMID 15260990.
- "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070. http://edoc.mpg.de/get.epl?fid=21592&did=275687&ver=0.
- "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Dev. Cell 9 (6): 791–804. 2006. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
- "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis". J. Cell Biol. 172 (2): 269–79. 2006. doi:10.1083/jcb.200508091. PMID 16418535.
- "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics". Exp. Cell Res. 312 (12): 2180–94. 2006. doi:10.1016/j.yexcr.2006.03.013. PMID 16630611.
- "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. 2006. doi:10.1038/nature04727. PMID 16710414. Bibcode: 2006Natur.441..315G.
- "Tuba stimulates intracellular N-WASP-dependent actin assembly". J. Cell Sci. 119 (Pt 13): 2715–26. 2006. doi:10.1242/jcs.03005. PMID 16757518.
- "Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination". J. Biol. Chem. 281 (39): 29042–53. 2006. doi:10.1074/jbc.M604025200. PMID 16885158.
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