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  • 标题:A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface
  • 本地全文:下载
  • 作者:Xiaohua Gong ; Amy Chang
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2001
  • 卷号:98
  • 期号:16
  • 页码:9104-9109
  • DOI:10.1073/pnas.161282998
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Pma1 is a plasma membrane H+-ATPase whose activity at the cell surface is essential for cell viability. In this paper we describe a temperature-sensitive pma1 allele, pma1-10 (with two point mutations in the first cytoplasmic loop of Pma1), in which the newly synthesized mutant protein fails to remain stable at the cell surface at 37{degrees}C. Instead, Pma1-10 appears to undergo internalization for vacuolar degradation in a manner dependent on End4, Vps27, Doa4, and Pep4. By contrast with wild-type Pma1, mutant Pma1-10 is hypophosphorylated and fails to associate with a Triton-insoluble fraction at 37{degrees}C, suggesting failure to enter lipid rafts. Kinetic analysis reveals that, at the permissive temperature, newly synthesized Pma1-10 acquires Triton-insolubility before becoming stabilized. We suggest that phosphorylation and lipid raft association may play important roles in maintaining protein stability at the plasma membrane.
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