The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Slc27a1  -  solute carrier family 27 (fatty acid...

Mus musculus

Synonyms: FATP-1, FATP1, Fatp, Fatp1, Fatty acid transport protein 1, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Slc27a1


High impact information on Slc27a1


Biological context of Slc27a1


Anatomical context of Slc27a1


Associations of Slc27a1 with chemical compounds

  • To correlate the expression of FATP to its physiological function, treatment of 3T3-L1 adipocytes with PPARgamma and RXRalpha activators resulted in an increased uptake of oleate [8].
  • Moreover, linoleic acid, a physiological ligand, up-regulated FATP expression 2-fold in a PPRE-dependent manner [8].
  • The very long chain acyl-CoA synthetase activity of the two enzymes was comparable as were the Km values for both ATP and coenzyme A. Interestingly, FATP1 was insensitive to inhibition by triacsin C, whereas ACS1 was inhibited by micromolar concentrations of the compound [9].
  • To investigate the role of FATP1 in glucose homeostasis and in the pathogenesis of insulin resistance, we examined the effect of acute lipid infusion or chronic high-fat feeding on insulin action in FATP1 KO mice [7].
  • These results are consistent with a mechanism of action for FATP involving ATP binding that is dependent on serine 250 of the IYTSGTTGXPK motif [12].

Regulatory relationships of Slc27a1

  • These results demonstrate that the FATP gene possesses a functional PPRE and is up-regulated by activators of PPARalpha and PPARgamma, thereby linking the activity of the protein to the expression of its gene [8].
  • In contrast, treatment with TNF-alpha inhibited basal and insulin-induced LCFA uptake and reduced FATP1 and -4 levels [13].

Other interactions of Slc27a1


Analytical, diagnostic and therapeutic context of Slc27a1

  • To address the enzymatic activity of the isolated protein, murine FATP1 and ACS1 were engineered to contain a C-terminal Myc-His tag expressed in COS1 cells via adenoviral-mediated infection and purified to homogeneity using nickel affinity chromatography [9].
  • Additionally, enhanced green fluorescent protein fusion constructs containing predicted membrane-associated or soluble portions of FATP1 were expressed in Cos7 cells and analyzed by immunofluorescence and subcellular fractionation [15].
  • Western blot analysis of 3T3-L1 adipocytes that natively express FATP1 demonstrate a prominent 130-kDa species as well as the expected 63-kDa FATP1, suggesting that this protein may participate in a cell surface transport protein complex [16].
  • Indirect immunofluorescence studies with selective permeabilization conditions and protease protection studies of sealed membrane vesicles from cells expressing epitope-tagged FATP1 were performed [15].
  • Fluorescence in situ hybridization analysis revealed that the murine FATP gene is localized to chromosome 8, band 8B3 [2].


  1. Cloning of wrinkle-free, a previously uncharacterized mouse mutation, reveals crucial roles for fatty acid transport protein 4 in skin and hair development. Moulson, C.L., Martin, D.R., Lugus, J.J., Schaffer, J.E., Lind, A.C., Miner, J.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Characterization of the murine fatty acid transport protein gene and its insulin response sequence. Hui, T.Y., Frohnert, B.I., Smith, A.J., Schaffer, J.E., Bernlohr, D.A. J. Biol. Chem. (1998) [Pubmed]
  3. Transgenic expression of fatty acid transport protein 1 in the heart causes lipotoxic cardiomyopathy. Chiu, H.C., Kovacs, A., Blanton, R.M., Han, X., Courtois, M., Weinheimer, C.J., Yamada, K.A., Brunet, S., Xu, H., Nerbonne, J.M., Welch, M.J., Fettig, N.M., Sharp, T.L., Sambandam, N., Olson, K.M., Ory, D.S., Schaffer, J.E. Circ. Res. (2005) [Pubmed]
  4. Impact on fatty acid metabolism and differential localization of FATP1 and FAT/CD36 proteins delivered in cultured human muscle cells. García-Martínez, C., Marotta, M., Moore-Carrasco, R., Guitart, M., Camps, M., Busquets, S., Montell, E., Gómez-Foix, A.M. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  5. Protein-mediated fatty acid uptake: novel insights from in vivo models. Doege, H., Stahl, A. Physiology (Bethesda, Md.) (2006) [Pubmed]
  6. Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein. Schaffer, J.E., Lodish, H.F. Cell (1994) [Pubmed]
  7. Inactivation of fatty acid transport protein 1 prevents fat-induced insulin resistance in skeletal muscle. Kim, J.K., Gimeno, R.E., Higashimori, T., Kim, H.J., Choi, H., Punreddy, S., Mozell, R.L., Tan, G., Stricker-Krongrad, A., Hirsch, D.J., Fillmore, J.J., Liu, Z.X., Dong, J., Cline, G., Stahl, A., Lodish, H.F., Shulman, G.I. J. Clin. Invest. (2004) [Pubmed]
  8. Identification of a functional peroxisome proliferator-responsive element in the murine fatty acid transport protein gene. Frohnert, B.I., Hui, T.Y., Bernlohr, D.A. J. Biol. Chem. (1999) [Pubmed]
  9. Characterization of the Acyl-CoA synthetase activity of purified murine fatty acid transport protein 1. Hall, A.M., Smith, A.J., Bernlohr, D.A. J. Biol. Chem. (2003) [Pubmed]
  10. Regulation of putative fatty acid transporters and Acyl-CoA synthetase in liver and adipose tissue in ob/ob mice. Memon, R.A., Fuller, J., Moser, A.H., Smith, P.J., Grunfeld, C., Feingold, K.R. Diabetes (1999) [Pubmed]
  11. FAT/CD36-mediated long-chain fatty acid uptake in adipocytes requires plasma membrane rafts. Pohl, J., Ring, A., Korkmaz, U., Ehehalt, R., Stremmel, W. Mol. Biol. Cell (2005) [Pubmed]
  12. Substitution of alanine for serine 250 in the murine fatty acid transport protein inhibits long chain fatty acid transport. Stuhlsatz-Krouper, S.M., Bennett, N.E., Schaffer, J.E. J. Biol. Chem. (1998) [Pubmed]
  13. Insulin causes fatty acid transport protein translocation and enhanced fatty acid uptake in adipocytes. Stahl, A., Evans, J.G., Pattel, S., Hirsch, D., Lodish, H.F. Dev. Cell (2002) [Pubmed]
  14. Liver fatty acid-binding protein gene ablation inhibits branched-chain fatty acid metabolism in cultured primary hepatocytes. Atshaves, B.P., McIntosh, A.M., Lyuksyutova, O.I., Zipfel, W., Webb, W.W., Schroeder, F. J. Biol. Chem. (2004) [Pubmed]
  15. Membrane topology of the murine fatty acid transport protein 1. Lewis, S.E., Listenberger, L.L., Ory, D.S., Schaffer, J.E. J. Biol. Chem. (2001) [Pubmed]
  16. Oligomerization of the murine fatty acid transport protein 1. Richards, M.R., Listenberger, L.L., Kelly, A.A., Lewis, S.E., Ory, D.S., Schaffer, J.E. J. Biol. Chem. (2003) [Pubmed]
WikiGenes - Universities