論文

査読有り 筆頭著者 責任著者
2014年7月

Unstable mutant lysozymes are degraded through the interaction with calnexin homolog Cne1p in Saccharomyces cerevisiae

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
  • Hiroyuki Azakami
  • ,
  • Masayoshi Uehara
  • ,
  • Ryohei Matsuo
  • ,
  • Yuta Tsurunaga
  • ,
  • Yuichiro Yamashita
  • ,
  • Masakatsu Usui
  • ,
  • Akio Kato

78
7
開始ページ
1263
終了ページ
1269
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1080/09168451.2014.918486
出版者・発行元
TAYLOR & FRANCIS LTD

Cne1p is a yeast homolog of calnexin, which is a constituent of endoplasmic reticulum (ER)-associated protein quality control system in mammals. Cne1p may be involved in the degradation of mis-folded lysozymes in Saccharomyces cerevisiae. To test this, c-Myc-tagged lysozymes were expressed in CNE1-deficient S. cerevisiae. The expression and secretion of an unstable lysozyme mutant G49N/D66H were enhanced and its intracellular localization was changed in the CNE1-deficient strain. Furthermore, when Cne1p was co-expressed with unstable lysozyme mutants (G49N/D66H, G49N/C76A, and K13D/G49N), its affinity to the misfolded mutant proteins was revealed by co-immunoprecipitation. The interaction with Cne1p was abrogated by the addition of tunicamycin, an inhibitor of N-glycosylation, indicating that N-linked carbohydrates might be necessary for protein binding to Cne1p. These results suggest that in yeasts, Cne1p interacts with misfolded lysozyme proteins possibly causing their retention in the ER and subsequent elimination via ER-associated degradation.

リンク情報
DOI
https://doi.org/10.1080/09168451.2014.918486
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000340209900026&DestApp=WOS_CPL
ID情報
  • DOI : 10.1080/09168451.2014.918486
  • ISSN : 0916-8451
  • eISSN : 1347-6947
  • Web of Science ID : WOS:000340209900026

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