期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 286, 期 28, 页码 25284-25290出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.244616
关键词
-
资金
- Human Frontiers Science Program [RGP0039/2007]
- European Research Council [ERC-2008-AdG 232648]
- Swedish Foundation for Strategic Research
- Swedish Cancer Foundation, the Swedish Cancer Foundation
- Natural Sciences and Engineering Research Council of Canada [9848]
- Lundbeck Foundation
Proteins interacting with membranes via a single hydrophobic segment can be classified as either monotopic or bitopic. Here, we probe the topology of a membrane-attached enzyme, the epsilon isoform of human diacylglycerol kinase (DGK epsilon), when inserted into rough microsomes and compare it with the monotopic membrane protein mouse caveolin-1. In contrast to previous findings, the N-terminal hydrophobic stretch in DGK epsilon attains a bitopic rather than a monotopic topology in our experimental system. In addition, we find that charged flanking residues as well as proline residues embedded in the hydrophobic segment are important determinants of monotopic versus bitopic topology.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据