FNBP1L

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Formin binding protein 1-like
Identifiers
Symbols FNBP1L ; C1orf39; TOCA1
External IDs Template:OMIM5 Template:MGI HomoloGene20898
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Formin binding protein 1-like, also known as FNBP1L, is a human gene.[1]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: FNBP1L formin binding protein 1-like".

Further reading

  • 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.
  • Katoh M, Katoh M (2004). "Identification and characterization of human FNBP1L gene in silico". Int. J. Mol. Med. 13 (1): 157–62. PMID 14654988.
  • 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.
  • Ho HY, Rohatgi R, Lebensohn AM; et al. (2004). "Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex". Cell. 118 (2): 203–16. doi:10.1016/j.cell.2004.06.027. PMID 15260990.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  • Itoh T, Erdmann KS, Roux A; et al. (2006). "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Dev. Cell. 9 (6): 791–804. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
  • Tsujita K, Suetsugu S, Sasaki N; et al. (2006). "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. doi:10.1083/jcb.200508091. PMID 16418535.
  • Aspenström P, Richnau N, Johansson AS (2006). "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. doi:10.1016/j.yexcr.2006.03.013. PMID 16630611.
  • Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
  • Kovacs EM, Makar RS, Gertler FB (2006). "Tuba stimulates intracellular N-WASP-dependent actin assembly". J. Cell. Sci. 119 (Pt 13): 2715–26. doi:10.1242/jcs.03005. PMID 16757518.
  • Kakimoto T, Katoh H, Negishi M (2006). "Regulation of neuronal morphology by Toca-1, an F-BAR/EFC protein that induces plasma membrane invagination". J. Biol. Chem. 281 (39): 29042–53. doi:10.1074/jbc.M604025200. PMID 16885158.

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