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  Quality control of protein complex assembly by a transmembrane recognition factor.

Natarajan, N., Foresti, O., Wendrich, K., Stein, A., & Carvalho, P. (2020). Quality control of protein complex assembly by a transmembrane recognition factor. Molecular Cell, 77(1), 108-119. doi:10.1016/j.molcel.2019.10.003.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-7B2E-F Version Permalink: http://hdl.handle.net/21.11116/0000-0005-7B35-6
Genre: Journal Article

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 Creators:
Natarajan, N., Author
Foresti, O., Author
Wendrich, K., Author
Stein, A.1, Author              
Carvalho, P., Author
Affiliations:
1Research Group of Membrane Protein Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_2149675              

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 Abstract: The inner nuclear membrane (INM) is continuous with the endoplasmic reticulum (ER) but harbors a distinctive proteome essential for nuclear functions. In yeast, the Asi1/Asi2/Asi3 ubiquitin ligase complex safeguards the INM proteome through the clearance of mislocalized ER membrane proteins. How the Asi complex selectively targets mislocalized proteins and coordinates its activity with other ER functions, such as protein biogenesis, is unclear. Here, we uncover a link between INM proteome identity and membrane protein complex assembly in the remaining ER. We show that lone proteins and complex subunits failing to assemble in the ER access the INM for Asi-mediated degradation. Substrates are recognized by direct binding of Asi2 to their transmembrane domains for subsequent ubiquitination by Asi1/Asi3 and membrane extraction. Our data suggest a model in which spatial segregation of membrane protein complex assembly and quality control improves assembly efficiency and reduces the levels of orphan subunits.

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Language(s): eng - English
 Dates: 2019-10-312020-01-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2019.10.003
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 77 (1) Sequence Number: - Start / End Page: 108 - 119 Identifier: -