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  Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1

Väth, K., Mattes, C., Reinhard, J., Covino, R., Stumpf, H., Hummer, G., et al. (2021). Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1. The Journal of Cell Biology, 220(8): e202011078. doi:10.1083/jcb.202011078.

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 Creators:
Väth, Kristina1, 2, Author
Mattes, Carsten1, 2, Author
Reinhard, John1, 2, Author
Covino, Roberto3, Author
Stumpf, Heike1, 2, Author
Hummer, Gerhard4, 5, Author                 
Ernst, Robert2, 3, Author
Affiliations:
1Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany, ou_persistent22              
2Preclinical Center for Molecular Signaling, Medical Faculty, Saarland University, Homburg, Germany, ou_persistent22              
3Frankfurt Institute of Advanced Sciences, Goethe-University, Frankfurt, German, ou_persistent22              
4Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
5Institute of Biophysics, Goethe-University, Frankfurt, Germany, ou_persistent22              

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 Abstract: The ER is a key organelle of membrane biogenesis and crucial for the folding of both membrane and secretory proteins. Sensors of the unfolded protein response (UPR) monitor the unfolded protein load in the ER and convey effector functions for maintaining ER homeostasis. Aberrant compositions of the ER membrane, referred to as lipid bilayer stress, are equally potent activators of the UPR. How the distinct signals from lipid bilayer stress and unfolded proteins are processed by the conserved UPR transducer Ire1 remains unknown. Here, we have generated a functional, cysteine-less variant of Ire1 and performed systematic cysteine cross-linking experiments in native membranes to establish its transmembrane architecture in signaling-active clusters. We show that the transmembrane helices of two neighboring Ire1 molecules adopt an X-shaped configuration independent of the primary cause for ER stress. This suggests that different forms of stress converge in a common, signaling-active transmembrane architecture of Ire1.

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Language(s): eng - English
 Dates: 2021-04-282020-11-122021-05-192021-07-012021-08-02
 Publication Status: Issued
 Pages: 17 + supplemental material
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1083/jcb.202011078
BibTex Citekey: vath_cysteine_2021
 Degree: -

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Title: The Journal of Cell Biology
  Other : JBC
Source Genre: Journal
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Publ. Info: New York, NY : Rockefeller Institute Press
Pages: - Volume / Issue: 220 (8) Sequence Number: e202011078 Start / End Page: - Identifier: ISSN: 0021-9525
CoNE: https://pure.mpg.de/cone/journals/resource/991042742946024_2