首页    期刊浏览 2024年11月05日 星期二
登录注册

文章基本信息

  • 标题:A C-terminal amphipathic helix is necessary for the in vivo tubule-shaping function of a plant reticulon
  • 作者:Emily Breeze ; Natasha Dzimitrowicz ; Verena Kriechbaumer
  • 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:2016
  • 卷号:113
  • 期号:39
  • 页码:10902-10907
  • DOI:10.1073/pnas.1605434113
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Reticulons (RTNs) are a class of endoplasmic reticulum (ER) membrane proteins that are capable of maintaining high membrane curvature, thus helping shape the ER membrane into tubules. The mechanism of action of RTNs is hypothesized to be a combination of wedging, resulting from the transmembrane topology of their conserved reticulon homology domain, and scaffolding, arising from the ability of RTNs to form low-mobility homo-oligomers within the membrane. We studied the plant RTN isoform RTN13, which has previously been shown to locate to ER tubules and the edges of ER cisternae and to induce constrictions in ER tubules when overexpressed, and identified a region in the C terminus containing a putative amphipathic helix (APH). Here we show that deletion of this region or disruption of the hydrophobic face of the predicted helix abolishes the ability of RTN13 to induce constrictions of ER tubules in vivo. These mutants, however, still retain their ability to interact and form low-mobility oligomers in the ER membrane. Hence, our evidence indicates that the conserved APH is a key structural feature for RTN13 function in vivo, and we propose that RTN, like other membrane morphogens, rely on APHs for their function.
  • 关键词:plant ; endoplasmic reticulum ; reticulon ; amphipathic helix ; membrane curvature
Loading...
联系我们|关于我们|网站声明
国家哲学社会科学文献中心版权所有