Cryo-EM structures of the endoplasmic reticulum membrane complex.
Cryo-EM structures of the endoplasmic reticulum membrane complex.
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DOI：
10.1111/febs.15786
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发表时间：
2022-01
期刊：
影响因子：
--
通讯作者：
Li H
中科院分区：
文献类型：
--
作者：
Bai L;Li H
The transmembrane α-helices of membrane proteins are in general highly hydrophobic, and they enter the lipid bilayer through a lateral gate in the Sec61 translocon. However, some transmembrane α-helices are less hydrophobic and form membrane channels or substrate-binding pockets. Insertion of these amphipathic transmembrane α-helices into the membrane requires the specific membrane-embedded insertase called the endoplasmic reticulum membrane complex (EMC), which is a multi-subunit chaperone distinct from the GET insertase complex. Four recent cryo-EM studies on the eukaryotic EMC have revealed their remarkable architectural conservation from yeast to human; a general consensus on the substrate transmembrane helix-binding pocket; and the evolutionary link to the prokaryotic insertases of the tail-anchored membrane proteins. These structures provide a solid framework for future mechanistic investigation. EMC has eight subunits in yeast and nine in human. EMC is a dual-function complex that inserts transmembrane domain of the tail-anchored proteins and chaperones biogenesis of multi-pass transmembrane proteins containing partially hydrophilic transmembrane helices. The EMC insertase and holdase activities are separable. The EMC structure contains two sizable cavities — a gated partially hydrophilic cavity and a lipid-filled hydrophobic cavity. Both cavities are involved in the EMC functions.
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