MassIVE MSV000082454

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Global proteome remodeling during ER stress involves Hac1-driven expression of long undecoded transcript isoforms

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Description

Cellular stress responses often require transcription-based activation of gene expression to promote cellular adaptation. Whether general mechanisms exist for stress-responsive gene down-regulation is less clear. A recently defined mechanism enables both up- and down-regulation of protein levels for distinct gene sets by the same transcription factor (TF) via coordinated induction of canonical mRNAs and long undecoded transcript isoforms (LUTIs). We analyzed parallel gene expression datasets to determine whether this mechanism contributes to the conserved Hac1-driven branch of the unfolded protein response (UPRER), indeed observing Hac1-dependent protein down-regulation accompanying the up-regulation of ER-related proteins that typifies UPRER activation. Proteins down-regulated by Hac1-driven LUTIs include those with electron transport chain (ETC) function. Abrogated ETC function improves the fitness of UPRER-activated cells, suggesting functional importance to this regulation. We conclude that the UPRER drives large-scale proteome remodeling, including coordinated up- and down-regulation of distinct protein classes, which is partly mediated by Hac1-induced LUTIs. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: TMT, LFQ, Unfolded Protein Response

Contact

Principal Investigators:
(in alphabetical order) 		Marko Jovanovic, Columbia University, USA
Submitting User: maki_vienna

Publications

Van Dalfsen KM, Hodapp S, Keskin A, Otto GM, Berdan CA, Higdon A, Cheunkarndee T, Nomura DK, Jovanovic M, Brar GA.
Global Proteome Remodeling during ER Stress Involves Hac1-Driven Expression of Long Undecoded Transcript Isoforms.
Dev. Cell. 2018 Jul 16;46(2):219-235.e8.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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