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Inefficient SRP Interaction with a Nascent Chain Triggers a mRNA Quality Control Pathway
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2014 (English)In: Cell, ISSN 0092-8674, E-ISSN 1097-4172, Vol. 156, no 1-2, 146-157 p.Article in journal (Refereed) Published
Abstract [en]

Misfolded proteins are often cytotoxic, unless cellular systems prevent their accumulation. Data presented here uncover a mechanism by which defects in secretory proteins lead to a dramatic reduction in their mRNAs and protein expression. When mutant signal sequences fail to bind to the signal recognition particle (SRP) at the ribosome exit site, the nascent chain instead contacts Argonaute2 (Ago2), and the mutant mRNAs are specifically degraded. Severity of signal sequence mutations correlated with increased proximity of Ago2 to nascent chain and mRNA degradation. Ago2 knockdown inhibited degradation of the mutant mRNA, while overexpression of Ago2 or knockdown of SRP54 promoted degradation of secretory protein mRNA. The results reveal a previously unappreciated general mechanismof translational quality control, in which specific mRNA degradation preemptively regulates aberrant protein production (RAPP).

Place, publisher, year, edition, pages
2014. Vol. 156, no 1-2, 146-157 p.
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Biochemistry and Molecular Biology Cell Biology
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URN: urn:nbn:se:su:diva-100858DOI: 10.1016/j.cell.2013.12.017ISI: 000329912200017OAI: oai:DiVA.org:su-100858DiVA: diva2:698225
Note

AuthorCount:13;

Available from: 2014-02-20 Created: 2014-02-17 Last updated: 2017-12-06Bibliographically approved

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Nilsson, IngMarievon Heijne, Gunnar
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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