Phosphorylation of Pal2 by the protein kinases Kin1 and Kin2 modulates HAC1 mRNA splicing in the unfolded protein response in yeast
| Autor: | Benjamin E. Turk, Jagadeesh Kumar Uppala, Leena Sathe, Chandrima Ghosh, Ashish Anshu, Madhusudan Dey, Charlotte I. Hammond, P. Raj Pokkuluri |
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| Rok vydání: | 2021 |
| Předmět: |
Untranslated region
Saccharomyces cerevisiae Proteins RNA Splicing Saccharomyces cerevisiae Protein Serine-Threonine Kinases Biochemistry Article RNA Messenger Phosphorylation Molecular Biology Messenger RNA Membrane Glycoproteins biology Chemistry Kinase Endoplasmic reticulum Membrane Proteins Cell Biology biology.organism_classification Cell biology Repressor Proteins Basic-Leucine Zipper Transcription Factors Unfolded Protein Response Unfolded protein response Signal transduction Protein Kinases |
| Zdroj: | Sci Signal |
| ISSN: | 1937-9145 1945-0877 |
| DOI: | 10.1126/scisignal.aaz4401 |
| Popis: | During cellular stress in the budding yeast Saccharomyces cerevisiae, an endoplasmic reticulum (ER)-resident dual kinase and RNase Ire1 splices an intron from HAC1 mRNA in the cytosol, thereby releasing its translational block. Hac1 protein then activates an adaptive cellular stress response called the unfolded protein response (UPR) that maintains ER homeostasis. The polarity-inducing protein kinases Kin1 and Kin2 contribute to HAC1 mRNA processing. Here, we showed that an RNA-protein complex that included the endocytic proteins Pal1 and Pal2 mediated HAC1 mRNA splicing downstream of Kin1 and Kin2. We found that Pal1 and Pal2 bound to the 3’-untranslated region (3’-UTR) of HAC1 mRNA, and a yeast strain lacking both Pal1 and Pal2 was deficient in HAC1 mRNA processing. We also showed that Kin1 and Kin2 directly phosphorylated Pal2, and that a non-phosphorylatable Pal2 mutant could not rescue the UPR defect in a pal1Δ pal2Δ strain. Thus, our work uncovers a Kin1/2-Pal2 signaling pathway that coordinates HAC1 mRNA processing and ER homeostasis. |
| Databáze: | OpenAIRE |
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