FNBP1L

From Wikipedia, the free encyclopedia


Formin binding protein 1-like
Identifiers
Symbol(s) FNBP1L; C1orf39; TOCA1
External IDs OMIM: 608848 MGI1925642 HomoloGene20898
Orthologs
Human Mouse
Entrez 54874 214459
Ensembl ENSG00000137942 ENSMUSG00000039735
Uniprot Q5T0N5 Q8K012
Refseq NM_001024948 (mRNA)
NP_001020119 (protein)
NM_153118 (mRNA)
NP_694758 (protein)
Location Chr 1: 93.69 - 93.79 Mb Chr 3: 122.53 - 122.58 Mb
Pubmed search [1] [2]

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]

[edit] References

[edit] 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.