Brefeldin A decreases the activity of the general amino acid permease [GAP1] and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae

• Autorzy: Alonso M , Burgos H.I. , Pannunzio V. , Hughes A.M. , Mattoon J.R. , Stella C.A.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

leucine permease; Brefeldin A agent; amino acid transport; antifungal agent; yeast cell; general amino acid permease; Saccharomyces cerevisiae

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2006
• Tom: 11
• Numer: 2
• Opis fizyczny: p.256-263,fig.,ref.

Twórcy

autor

Alonso M

• University of Buenos Aires, Paraguay 2155, 5 Piso, Argentina

autor

Burgos H.I.

autor

Pannunzio V.

autor

Hughes A.M.

autor

Mattoon J.R.

autor

Stella C.A.

Bibliografia

• 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. 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. Schreve, J. and Garrett, 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. 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. 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. 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. 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. 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. 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. 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. Shah, N. and Klausner, R.D. Brefeldin A reversibly inhibits secretion in Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993) 5345-5348.
• 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. 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. 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. 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. 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. Vallejo, C.G. and Serrano, R. Physiology of mutants with reduced expression of plasma membrane H+-ATPase. Yeast 5 (1989) 307-319.