Structural insights into the membrane chaperones for multi-pass membrane protein biogenesis.
Structural insights into the membrane chaperones for multi-pass membrane protein biogenesis.
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DOI：
10.1016/j.sbi.2023.102563
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发表时间：
2023-02
影响因子：
6.8
通讯作者：
Lin Bai;Huilin Li
中科院分区：
文献类型：
--
作者：
Lin Bai;Huilin Li
Certain transmembrane α-helices of multi-pass membrane proteins line substrate transport paths or catalytic pockets and, therefore, are partially hydrophilic. Sec61 alone is insufficient to insert these less hydrophobic segments into the membrane and needs to work with dedicated membrane chaperones. Three such membrane chaperones have been described in the literature—the endoplasmic reticulum membrane protein complex (EMC), the TMCO1 complex, and the PAT complex. Recent structural studies on these membrane chaperones have revealed their overall architecture, multi-subunit assembly, putative substrate transmembrane helix-binding pockets, and cooperative mechanisms with the ribosome and Sec61 translocon. These structures are providing initial insights into the poorly understood processes of multi-pass membrane protein biogenesis.
