Molecules and Cells

, Volume 31, Issue 2, pp 151–158

Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome

  • Ki-Hyun Kim
  • Eun-Kyung Kim
  • Su-Jin Kim
  • Yun-Hee Park
  • Park Hee-Moon
Article

DOI: 10.1007/s10059-011-0012-z

Cite this article as:
Kim, KH., Kim, EK., Kim, SJ. et al. Mol Cells (2011) 31: 151. doi:10.1007/s10059-011-0012-z
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Abstract

To study the effect of the ret1-1 mutation on the secretome, the glycosylation patterns and locations of the secretory proteins and glycosyltransferases responsible for glycosylation were investigated. Analyses of secretory proteins and cell wall-associated glycoproteins showed severe impairment of glycosylation in this mutant. Results from 2D-polyacrylamide gel electrophoresis (PAGE) indicated defects in the glycosylation and cellular localization of SDS-soluble cell wall proteins. Localization of RFP-tagged glycosyltransferase proteins in ret1-1 indicated an impairment of Golgi-to retrograde transport at a non-permissive temperature. Thus, impaired glycosylation caused by the mislocalization of ER resident proteins appears to be responsible for the alterations in the secretome and the increased sensitivity to ER stress in ret1-1 mutant cells.

Keywords

glycosylation localization ret1-1 mutation Saccharomyces cerevisiae secretome 

Copyright information

© The Korean Society for Molecular and Cellular Biology and Springer Netherlands 2011

Authors and Affiliations

  • Ki-Hyun Kim
    • 1
  • Eun-Kyung Kim
    • 1
  • Su-Jin Kim
    • 1
  • Yun-Hee Park
    • 1
  • Park Hee-Moon
    • 1
  1. 1.Department of Microbiology and Molecular Biology, College of Bioscience and BiotechnologyChungnam National UniversityDaejeonKorea

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