Membrane-protein integration and the role of the translocation channel - PubMed (original) (raw)
Review
Membrane-protein integration and the role of the translocation channel
Tom A Rapoport et al. Trends Cell Biol. 2004 Oct.
Abstract
Most eukaryotic membrane proteins are integrated into the lipid bilayer during their synthesis at the endoplasmic reticulum (ER). Their integration occurs with the help of a protein-conducting channel formed by the heterotrimeric Sec61 membrane-protein complex. The crystal structure of an archaeal homolog of the complex suggests mechanisms that enable the channel to open across the membrane and to release laterally hydrophobic transmembrane segments of nascent membrane proteins into lipid. Many aspects of membrane-protein integration remain controversial and poorly understood, but new structural data provide testable hypotheses. We propose a model of how the channel recognizes transmembrane segments, orients them properly with respect to the plane of the membrane and releases them into lipid. We also discuss how the channel would prevent small molecules from crossing the lipid bilayer while it is integrating proteins.
Similar articles
- Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.
Rapoport TA. Rapoport TA. Nature. 2007 Nov 29;450(7170):663-9. doi: 10.1038/nature06384. Nature. 2007. PMID: 18046402 Review. - Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane.
Heinrich SU, Rapoport TA. Heinrich SU, et al. EMBO J. 2003 Jul 15;22(14):3654-63. doi: 10.1093/emboj/cdg346. EMBO J. 2003. PMID: 12853480 Free PMC article. - Structural determinants of lateral gate opening in the protein translocon.
Gumbart J, Schulten K. Gumbart J, et al. Biochemistry. 2007 Oct 2;46(39):11147-57. doi: 10.1021/bi700835d. Epub 2007 Aug 31. Biochemistry. 2007. PMID: 17760424 - Aggregation and porin-like channel activity of a beta sheet peptide.
Thundimadathil J, Roeske RW, Jiang HY, Guo L. Thundimadathil J, et al. Biochemistry. 2005 Aug 2;44(30):10259-70. doi: 10.1021/bi0508643. Biochemistry. 2005. PMID: 16042403 - Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring.
de Planque MR, Killian JA. de Planque MR, et al. Mol Membr Biol. 2003 Oct-Dec;20(4):271-84. doi: 10.1080/09687680310001605352. Mol Membr Biol. 2003. PMID: 14578043 Review.
Cited by
- Key contributions of a glycolipid to membrane protein integration.
Shimamoto K, Fujikawa K, Osawa T, Mori S, Nomura K, Nishiyama KI. Shimamoto K, et al. Proc Jpn Acad Ser B Phys Biol Sci. 2024;100(7):387-413. doi: 10.2183/pjab.100.026. Proc Jpn Acad Ser B Phys Biol Sci. 2024. PMID: 39085064 Free PMC article. Review. - Interaction between glycolipid MPIase and proteinaceous factors during protein integration into the cytoplasmic membrane of E. coli.
Nishikawa H, Sawasato K, Mori S, Fujikawa K, Nomura K, Shimamoto K, Nishiyama KI. Nishikawa H, et al. Front Mol Biosci. 2022 Aug 19;9:986602. doi: 10.3389/fmolb.2022.986602. eCollection 2022. Front Mol Biosci. 2022. PMID: 36060260 Free PMC article. Review. - Role of a bacterial glycolipid in Sec-independent membrane protein insertion.
Nomura K, Mori S, Fujikawa K, Osawa T, Tsuda S, Yoshizawa-Kumagaye K, Masuda S, Nishio H, Yoshiya T, Yoda T, Shionyu M, Shirai T, Nishiyama KI, Shimamoto K. Nomura K, et al. Sci Rep. 2022 Jul 18;12(1):12231. doi: 10.1038/s41598-022-16304-1. Sci Rep. 2022. PMID: 35851412 Free PMC article. - Doing What Spiders Cannot-A Road Map to Supreme Artificial Silk Fibers.
Johansson J, Rising A. Johansson J, et al. ACS Nano. 2021 Feb 23;15(2):1952-1959. doi: 10.1021/acsnano.0c08933. Epub 2021 Jan 20. ACS Nano. 2021. PMID: 33470789 Free PMC article. - Ribosome-associated quality control of membrane proteins at the endoplasmic reticulum.
Phillips BP, Miller EA. Phillips BP, et al. J Cell Sci. 2020 Nov 27;133(22):jcs251983. doi: 10.1242/jcs.251983. J Cell Sci. 2020. PMID: 33247003 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources