期刊
CELL
卷 138, 期 3, 页码 549-561出版社
CELL PRESS
DOI: 10.1016/j.cell.2009.05.025
关键词
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资金
- American Heart Association
- Intramural Research Programs of the NINDS
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Institutes of Health
- Howard Hughes Medical Institute investigator
The endoplasmic reticulum ( ER) consists of tubules that are shaped by the reticulons and DP1/Yop1p, but how the tubules form an interconnected network is unknown. Here, we show that mammalian atlastins, which are dynamin-like, integral membrane GTPases, interact with the tubule-shaping proteins. The atlastins localize to the tubular ER and are required for proper network formation in vivo and in vitro. Depletion of the atlastins or overexpression of dominant-negative forms inhibits tubule interconnections. The Sey1p GTPase in S. cerevisiae is likely a functional ortholog of the atlastins; it shares the same signature motifs and membrane topology and interacts genetically and physically with the tubule-shaping proteins. Cells simultaneously lacking Sey1p and a tubule-shaping protein have ER morphology defects. These results indicate that formation of the tubular ER network depends on conserved dynamin-like GTPases. Since atlastin-1 mutations cause a common form of hereditary spastic paraplegia, we suggest ER-shaping defects as a neuropathogenic mechanism.
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