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Gene Review

ACB1  -  long-chain fatty acid transporter ACB1

Saccharomyces cerevisiae S288c

Synonyms: ACB, ACBP, Acyl-CoA-binding protein, YGR037C
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Disease relevance of ACB1

  • Muller cells may secrete ACBP in the inner plexiform layer, thereby decreasing the sensitivity of GABA(A) receptors expressed on the surface of ganglion cell dendrites [1].

High impact information on ACB1

  • Much work on the biochemical properties regarding the ACBP has been performed using various vertebrate and plant tissues, as well as different types of cells in culture, the regulatory mechanisms underlying ACBP gene expression have remained poorly understood [2].
  • A conditional knockout strain (Y700pGAL1-ACB1) with the ACB1 gene under control of the GAL1 promoter exhibited an altered acyl-CoA profile with a threefold increase in the relative content of C18:0-CoA, without affecting total acyl-CoA level as previously reported for an adapted acb1Delta strain [3].
  • The plasma membrane of the Acb1p-depleted strain contained increased levels of inositol-phosphoceramide and mannose-inositol-phosphoceramide and lysophospholipids [3].
  • Unsaturated fatty acid repression of OLE1 transcription, however, is not affected by the disrupted ACBP gene [4].
  • Despite the fact that the stearoyl-CoA concentration was increased 7-fold and the Delta9-desaturase mRNA level was increased 3-fold, the synthesis of oleic acid was unchanged in the acb1-disrupted strain [5].

Biological context of ACB1


Anatomical context of ACB1

  • Mass spectrometric analysis revealed a dramatic reduction in the content of ceramides in whole-cell lipids and in vacuoles isolated from Acb1p-depleted cells [9].
  • ACBP does not cross the blood-brain barrier [1].
  • ACBP was localized to Muller glial cells by hybridization histochemistry and by immunohistochemistry [1].
  • The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved [10].

Associations of ACB1 with chemical compounds

  • The heterologously expressed bovine ACBP constituted up to 6.4% of total cellular protein and the processing was identical with that of native bovine ACBP, i.e. the initiating methionine was removed and the following serine residue was N-acetylated [11].
  • We suggest that the reduced ceramide synthesis in Acb1p-depleted cells leads to severely altered vacuole morphology, perturbed vacuole assembly and strong inhibition of homotypic vacuole fusion [9].
  • The interaction was also confirmed by a "pull-down" assay in which histidine-tagged ACBP was used to pull down the GABA(A)alpha1 [1].
  • Acyl-CoA-binding protein (ACBP) mRNA was one of four mRNAs selected by this screen, the proteins of which interact with GABA receptors [1].

Other interactions of ACB1

  • The fact that Gas1p maturation is unaffected by Acb1p depletion, despite the lowered ceramide content in these cells, indicates that ceramide synthesis in yeast could be compartmentalized [9].

Analytical, diagnostic and therapeutic context of ACB1


  1. Activity-dependent expression of acyl-coenzyme a-binding protein in retinal muller glial cells evoked by optokinetic stimulation. Barmack, N.H., Bilderback, T.R., Liu, H., Qian, Z., Yakhnitsa, V. J. Neurosci. (2004) [Pubmed]
  2. Isolation and characterization of a humoral factor that stimulates transcription of the acyl-CoA-binding protein in the pheromone gland of the silkmoth, Bombyx mori. Ohnishi, A., Koshino, H., Takahashi, S., Esumi, Y., Matsumoto, S. J. Biol. Chem. (2005) [Pubmed]
  3. Depletion of acyl-coenzyme A-binding protein affects sphingolipid synthesis and causes vesicle accumulation and membrane defects in Saccharomyces cerevisiae. Gaigg, B., Neergaard, T.B., Schneiter, R., Hansen, J.K., Faergeman, N.J., Jensen, N.A., Andersen, J.R., Friis, J., Sandhoff, R., Schrøder, H.D., Knudsen, J. Mol. Biol. Cell (2001) [Pubmed]
  4. Regulatory elements that control transcription activation and unsaturated fatty acid-mediated repression of the Saccharomyces cerevisiae OLE1 gene. Choi, J.Y., Stukey, J., Hwang, S.Y., Martin, C.E. J. Biol. Chem. (1996) [Pubmed]
  5. Disruption of the gene encoding the acyl-CoA-binding protein (ACB1) perturbs acyl-CoA metabolism in Saccharomyces cerevisiae. Schjerling, C.K., Hummel, R., Hansen, J.K., Borsting, C., Mikkelsen, J.M., Kristiansen, K., Knudsen, J. J. Biol. Chem. (1996) [Pubmed]
  6. Saccharomyces carlsbergensis contains two functional genes encoding the acyl-CoA binding protein, one similar to the ACB1 gene from S. cerevisiae and one identical to the ACB1 gene from S. monacensis. Børsting, C., Hummel, R., Schultz, E.R., Rose, T.M., Pedersen, M.B., Knudsen, J., Kristiansen, K. Yeast (1997) [Pubmed]
  7. Yeast acyl-CoA-binding protein: acyl-CoA-binding affinity and effect on intracellular acyl-CoA pool size. Knudsen, J., Faergeman, N.J., Skøtt, H., Hummel, R., Børsting, C., Rose, T.M., Andersen, J.S., Højrup, P., Roepstorff, P., Kristiansen, K. Biochem. J. (1994) [Pubmed]
  8. Evolution of the acyl-CoA binding protein (ACBP). Burton, M., Rose, T.M., Faergeman, N.J., Knudsen, J. Biochem. J. (2005) [Pubmed]
  9. Acyl-CoA-binding protein, Acb1p, is required for normal vacuole function and ceramide synthesis in Saccharomyces cerevisiae. Faergeman, N.J., Feddersen, S., Christiansen, J.K., Larsen, M.K., Schneiter, R., Ungermann, C., Mutenda, K., Roepstorff, P., Knudsen, J. Biochem. J. (2004) [Pubmed]
  10. Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family. Costabel, M.D., Erm??cora, M.R., Santom??, J.A., Alzari, P.M., Gu??rin, D.M. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  11. Effect of heterologous expression of acyl-CoA-binding protein on acyl-CoA level and composition in yeast. Mandrup, S., Jepsen, R., Skøtt, H., Rosendal, J., Højrup, P., Kristiansen, K., Knudsen, J. Biochem. J. (1993) [Pubmed]
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