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. 1988 Jun;170(6):2654–2658. doi: 10.1128/jb.170.6.2654-2658.1988

Derepression of high-affinity glucose uptake requires a functional secretory system in Saccharomyces cerevisiae.

L F Bisson 1
PMCID: PMC211184  PMID: 3286616

Abstract

The expression of high-affinity glucose uptake in Saccharomyces cerevisiae strains carrying conditional mutations conferring a block of secretion and cell surface growth (sec) revealed a requirement for a functional secretory pathway for derepression of carrier activity. Thus, in strains carrying the sec1-1, sec4-2, sec7-1, sec14-3, or sec17-1 mutation, no high-affinity carrier activity was expressed after a shift to derepressing glucose concentrations at the nonpermissive temperature. In the case of sec18-1, however, derepression of carrier activity did occur at both the permissive and nonpermissive temperature, but not to the same extent as found in the wild-type strain, suggesting that SEC18 function may not be essential for expression of carrier activity. In sec1-1, accumulation of high-affinity carrier activity (or a component thereof) in presecretory vesicles during incubation at the nonpermissive temperature was demonstrated. The presence of a high glucose concentration in the medium did not affect transfer of that accumulated carrier function to the cell surface. Carrier function did not accumulate in strains carrying the other sec mutations. Analysis of the stability of high-affinity carrier activity at 37 degrees C demonstrated rapid and unexpected loss of carrier activity not affected by the presence of glucose in the medium. Thus, blockage of cell surface growth seems to affect turnover rates of hexose carrier activities.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alonso A., Kotyk A. Apparent half-lives of sugar transport proteins in Saccharomyces cerevisiae. Folia Microbiol (Praha) 1978;23(2):118–125. doi: 10.1007/BF02915311. [DOI] [PubMed] [Google Scholar]
  2. Bisson L. F., Fraenkel D. G. Expression of kinase-dependent glucose uptake in Saccharomyces cerevisiae. J Bacteriol. 1984 Sep;159(3):1013–1017. doi: 10.1128/jb.159.3.1013-1017.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bisson L. F., Fraenkel D. G. Involvement of kinases in glucose and fructose uptake by Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1730–1734. doi: 10.1073/pnas.80.6.1730. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bisson L. F., Fraenkel D. G. Transport of 6-deoxyglucose in Saccharomyces cerevisiae. J Bacteriol. 1983 Sep;155(3):995–1000. doi: 10.1128/jb.155.3.995-1000.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bisson L. F., Neigeborn L., Carlson M., Fraenkel D. G. The SNF3 gene is required for high-affinity glucose transport in Saccharomyces cerevisiae. J Bacteriol. 1987 Apr;169(4):1656–1662. doi: 10.1128/jb.169.4.1656-1662.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Busturia A., Lagunas R. Catabolite inactivation of the glucose transport system in Saccharomyces cerevisiae. J Gen Microbiol. 1986 Feb;132(2):379–385. doi: 10.1099/00221287-132-2-379. [DOI] [PubMed] [Google Scholar]
  7. Ferro-Novick S., Novick P., Field C., Schekman R. Yeast secretory mutants that block the formation of active cell surface enzymes. J Cell Biol. 1984 Jan;98(1):35–43. doi: 10.1083/jcb.98.1.35. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Lagunas R., DeJuan C., Benito B. Inhibition of biosynthesis of Saccharomyces cerevisiae sugar transport system by tunicamycin. J Bacteriol. 1986 Dec;168(3):1484–1486. doi: 10.1128/jb.168.3.1484-1486.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Neigeborn L., Schwartzberg P., Reid R., Carlson M. Null mutations in the SNF3 gene of Saccharomyces cerevisiae cause a different phenotype than do previously isolated missense mutations. Mol Cell Biol. 1986 Nov;6(11):3569–3574. doi: 10.1128/mcb.6.11.3569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Novick P., Field C., Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 1980 Aug;21(1):205–215. doi: 10.1016/0092-8674(80)90128-2. [DOI] [PubMed] [Google Scholar]
  11. Novick P., Schekman R. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1858–1862. doi: 10.1073/pnas.76.4.1858. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Walworth N. C., Novick P. J. Purification and characterization of constitutive secretory vesicles from yeast. J Cell Biol. 1987 Jul;105(1):163–174. doi: 10.1083/jcb.105.1.163. [DOI] [PMC free article] [PubMed] [Google Scholar]

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