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Global Proteome Remodeling during ER Stress Involves Hac1-Driven Expression of Long Undecoded Transcript Isoforms.
Kelsey Marie Van Dalfsen1, Stefanie Hodapp2, Abdurrahman Keskin2
1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Developmental Cell
|July 18, 2018
Summary
Cellular stress responses can involve gene downregulation. This study reveals that the unfolded protein response (UPRER) uses long undecoded transcript isoforms (LUTIs) to downregulate proteins, including those in the electron transport chain (ETC).
Area of Science:
- Cellular Biology
- Molecular Biology
- Genetics
Background:
- Cellular stress responses typically involve gene activation for adaptation.
- Mechanisms for stress-induced gene downregulation are less understood.
- A novel mechanism coordinates mRNA and long undecoded transcript isoforms (LUTIs) for protein level regulation.
Purpose of the Study:
- To investigate if LUTIs contribute to the Hac1-driven unfolded protein response (UPRER).
- To determine if UPRER involves coordinated protein upregulation and downregulation.
- To explore the functional significance of Hac1-mediated protein downregulation.
Main Methods:
- Analysis of parallel gene expression datasets.
- Investigating Hac1-dependent gene expression.
- Assessing protein levels and cellular fitness under UPRER conditions.
Main Results:
- Hac1-dependent protein downregulation was observed during UPRER activation.
- Proteins involved in electron transport chain (ETC) function were downregulated by Hac1-induced LUTIs.
- Impaired ETC function enhanced the fitness of UPRER-activated cells.
Conclusions:
- The UPRER orchestrates large-scale proteome remodeling.
- Hac1-induced LUTIs mediate coordinated upregulation of ER proteins and downregulation of other protein classes, such as ETC components.
- This coordinated regulation is crucial for cellular adaptation during UPRER.
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