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Brefeldin a decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae


Brefeldin A is a commonly used antifungal agent that reversibly blocks protein transport from the endoplasmic reticulum to the Golgi complex. In this study, we aimed to characterize L-leucine uptake in Saccharomyces cerevisiae in the presence of brefeldin A. For this purpose, we used a synthetic medium, containing L-proline and the detergent SDS, which allows the agent to permeate into the yeast cell. The results obtained with a wild type strain and a gap1 mutant indicate that BFA causes either direct or indirect modification of the transport and/or processing of L-leucine permeases. The presence of BFA affects the kinetic parameter values for L-leucine uptake and decreases not only the uptake mediated by the general system (GAP1), but also that through the specific BAP2 (S1) and/or S2 systems.



amino acid permease


branched-chain amino acid permease 2


brefeldin A


endoplasmic reticulum


general amino acid permease


Golgi complex

S1 and S2:

specific L-leucine transport systems


  1. 1.

    Grenson, M. Amino acid transporters in yeast: structure, function and regulation. Molecular Aspects of Transport Proteins. Elsevier, Amsterdam; New York. 1992, 219–245.

  2. 2.

    Regenberg, B., Holmberg, S. and Kiellandt-Brandt, M. Functional analysis of amino acid permeases in yeast. XVth SMYTE (Small Meeting in Yeast Transport) Mexico, 1997, Abstr. 33.

  3. 3.

    Schreve, J. and Garett, J.M. The branched-chain amino acid permease gene of Saccharomyces cerevisiae, BAP2, encodes the high-affinity leucine permease (S1). Yeast 13 (1997) 435–439.

  4. 4.

    Kotliar, N., Stella, C.A., Ramos, E.H. and Mattoon, J.R. L-leucine transport systems in Saccharomyces cerevisiae. Participation of GAP1, S1 and S2 transport systems. Cell. Mol. Biol. 40 (1994) 833–842.

  5. 5.

    Bennett, M.K. and Scheller, R.H. The molecular machinery for secretion is conserved from yeast to neurons. Proc. Natl. Acad. Sci. USA 90 (1993) 2559–2563.

  6. 6.

    Roberg, K.J., Bickel, S., Rowley, N. and Kaiser, C.A. Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8. Genetics 147 (1997) 1569–1584.

  7. 7.

    Beck, T., Schmidt, A. and Hall, M.N. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J. Cell. Biol. 146 (1999) 1227–1238.

  8. 8.

    Chen, E.J. and Kaiser, C.A. Amino acids regulate the intracellular trafficking of the general amino acid permease of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 99 (2002) 14837–14842

  9. 9.

    Umebayashi, K. and Nakano, A. Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J. Cell. Biol. 161 (2003) 1117–1131.

  10. 10.

    Graham, T.R., Scott, P.A. and Emr, S.D. Brefeldin A reversibly blocks early but not late protein transport steps in the yeast secretory pathway. EMBO J. 12 (1993) 869–877.

  11. 11.

    Shah, N. and Klausner, R.D. Brefeldin A reversibly inhibits secretion in Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 5345–5348.

  12. 12.

    Vogel, J.P., Lee, J.N., Kirsch, D.R., Rose, M.D. and Sztul, M.D. Brefeldin A causes a defect in secretion in Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 3040–3043.

  13. 13.

    Crespo, P.M., Iglesias-Bartolome, R. and Daniotti, J.L. Ganglioside GD3 traffics from the trans-Golgi network to plasma membrane by a Rab11-independent and brefeldin A-insensitive exocytic pathway. J. Biol. Chem. 279 (2004) 47610–47618.

  14. 14.

    Pannunzio, V.G., Burgos, H.I., Alonso, M., Mattoon, J.R., Ramos, E.H. and Stella, C.A. A Simple Chemical Method for Rendering Wild-Type Yeast Permeable to Brefeldin A That Does Not Require the Presence of an erg6 Mutation. J. Biomed. Biotechnol. 3 (2004) 150–155.

  15. 15.

    Grenson, M., Hou, C. and Crabeel, M. Multiplicity of the amino acid permeases in Saccharomyces cerevisiae. IV. Evidence for a general amino acid permease. J. Bacteriol. 103 (1970) 770–777.

  16. 16.

    Shimoni, Y., Kurihara, T., Ravazzola, M., Amherdt, M., Orci, L. and Schekman, R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J. Cell Biol. 151 (2000) 973–984.

  17. 17.

    Vallejo, C.G. and Serrano, R. Physiology of mutants with reduced expression of plasma membrane H+-ATPase. Yeast 5 (1989) 307–319.

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Correspondence to Carlos A. Stella.

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Alonso, M., Burgos, H.I., Pannunzio, V. et al. Brefeldin a decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae . Cell. Mol. Biol. Lett. 11, 256–263 (2006).

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Key words

  • Brefeldin A
  • Leucine permeases
  • Saccharomyces cerevisiae