期刊
MOLECULAR CELL
卷 68, 期 4, 页码 673-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2017.10.022
关键词
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资金
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- NIH, National Institute of General Medical Sciences [P41GM103393]
- NIH [1 S10 OD016232-01, 1 S10 OD021505-01, 1 U54 DK110858-01, GM115129, T32GM007464, T32HL007576]
- Nora Eccles Treadwell Foundation
- Howard Hughes Medical Institute
- AHA [14POST20380216]
- NIH Research Training in Hematology grant [T32DK007115]
Vms1 translocates to damaged mitochondria in response to stress, whereupon its binding partner, Cdc48, contributes to mitochondrial protein homeostasis. Mitochondrial targeting of Vms1 is mediated by its conserved mitochondrial targeting domain (MTD), which, in unstressed conditions, is inhibited by intramolecular binding to the Vms1 leucine-rich sequence (LRS). Here, we report a 2.7 angstrom crystal structure of Vms1 that reveals that the LRS lies in a hydrophobic groove in the autoinhibited MTD. We also demonstrate that the oxidized sterol, ergosterol peroxide, is necessary and sufficient for Vms1 localization to mitochondria, through binding the MTD in an interaction that is competitive with binding to the LRS. These data support a model in which stressed mitochondria generate an oxidized sterol receptor that recruits Vms1 to support mitochondrial protein homeostasis.
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