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  The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins

Shurtleff, M. J., Itzhak, D. N., Hussmann, J. A., Oakdale, N. T. S., Costa, E. A., Jonikas, M., et al. (2018). The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins. eLife, 7: e37018. doi:10.7554/eLife.37018.

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© 2018, Shurtleff et al.

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 Creators:
Shurtleff, Matthew J.1, Author
Itzhak, Daniel N.2, Author              
Hussmann, Jeffrey A.1, Author
Oakdale, Nicole T. Schirle1, Author
Costa, Elizabeth A.1, Author
Jonikas, Martin1, Author
Weibezahn, Jimena1, Author
Popova, Katerina D.1, Author
Jan, Calvin H.1, Author
Sinitcyn, Pavel2, Author              
Vembar, Shruthi S.1, Author
Hernandez, Hilda1, Author
Cox, Jürgen3, Author              
Burlingame, Alma L.1, Author
Brodsky, Jeffrey1, Author
Frost, Adam1, Author
Borner, Georg H. H.4, Author              
Weissman, Jonathan S.1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3Cox, Jürgen / Computational Systems Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_2063284              
4Borner, Georg / Systems Biology of Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_3060205              

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Free keywords: ENDOPLASMIC-RETICULUM; SACCHAROMYCES-CEREVISIAE; SHOTGUN PROTEOMICS; CYSTIC-FIBROSIS; IDENTIFICATION; CRISPR; MUTATIONS; DISEASE; SCREEN; VIRUSLife Sciences & Biomedicine - Other Topics;
 Abstract: The endoplasmic reticulum (ER) supports biosynthesis of proteins with diverse transmembrane domain (TMD) lengths and hydrophobicity. Features in transmembrane domains such as charged residues in ion channels are often functionally important, but could pose a challenge during cotranslational membrane insertion and folding. Our systematic proteomic approaches in both yeast and human cells revealed that the ER membrane protein complex (EMC) binds to and promotes the biogenesis of a range of multipass transmembrane proteins, with a particular enrichment for transporters. Proximity-specific ribosome profiling demonstrates that the EMC engages clients cotranslationally and immediately following clusters of TMDs enriched for charged residues. The EMC can remain associated after completion of translation, which both protects clients from premature degradation and allows recruitment of substrate-specific and general chaperones. Thus, the EMC broadly enables the biogenesis of multipass transmembrane proteins containing destabilizing features, thereby mitigating the trade-off between function and stability.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 23
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000434765900001
DOI: 10.7554/eLife.37018
 Degree: -

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Project name : European Research Council (ERC2012-SyG_318987-ToPAG)
Grant ID : 318987
Funding program : -
Funding organization : European Commission (EC)

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 7 Sequence Number: e37018 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X