4.8 Article

Dynamic membrane topology in an unassembled membrane protein

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NATURE CHEMICAL BIOLOGY
卷 15, 期 10, 页码 945-+

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NATURE PUBLISHING GROUP
DOI: 10.1038/s41589-019-0356-9

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资金

  1. Knut and Alice Wallenberg Foundation [2012.0282]
  2. Swedish Research Council [621-2014-3713]
  3. Swedish Cancer Foundation [15 0888]
  4. EMBO/Marie Curie Actions [ALTF 211-2014]
  5. HFSP [LT000277/2015-L]

向作者/读者索取更多资源

Helical membrane proteins are typically assumed to attain stable transmembrane topologies immediately upon co-translational membrane insertion. Here we show that unassembled monomers of the small multidrug resistance (SMR) family exist in a dynamic equilibrium where the N-terminal transmembrane helix flips in and out of the membrane, with rates that depend on dimerization and the polypeptide sequence. Thus, membrane topology can display rapid dynamics in vivo and can be regulated by post-translational assembly.

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