期刊
NATURE METABOLISM
卷 1, 期 9, 页码 876-885出版社
NATURE RESEARCH
DOI: 10.1038/s42255-019-0111-2
关键词
-
资金
- NIH [DK107397, DK109888, DK110656, DK112826, DK108833, DK115824, DK116450, DK103930, AR066660, AR070200, HL129362, DK091317]
- American Heart Association [18PRE33960491, 19PRE34380991]
- Larry H. & Gail Miller Family Foundation
- Uehara Memorial Foundation
- Washington University in St. Louis [P30 DK020579]
- [S10 OD016232]
- [S10 OD021505]
- [U54 DK110858]
The biophysical environment of membrane phospholipids affects the structure, function, and stability of membrane-bound proteins(1,2). Obesity can disrupt membrane lipids, and, in particular, alter the activity of sarco-endoplasmic reticulum Ca2+-ATPase (SERCA) to affect cellular metabolism(3-5). Recent evidence suggests that the transport efficiency (Ca2+ uptake and ATP hydrolysis) of skeletal muscle SERCA can be uncoupled to increase energy expenditure and protect mice from diet-induced obesity(6,7). In isolated sarcoplasmic reticulum vesicles, membrane phospholipid composition is known to modulate SERCA efficiency(8-11). Here we show that skeletal muscle sarcoplasmic reticulum phospholipids can be altered to decrease SERCA efficiency and increase the whole-body metabolic rate. The absence of skeletal muscle phosphatidylethanolamine methyltransferase (PEMT) promotes an increase in the skeletal muscle and whole-body metabolic rate to protect mice from diet-induced obesity. The elevation in metabolic rate is caused by a decrease in SERCA Ca2+-transport efficiency, whereas mitochondrial uncoupling is unaffected. Our findings support the hypothesis that skeletal muscle energy efficiency can be reduced to promote protection from obesity.
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