Phosphorylation of Pal2 by the Protein Kinases Kin1 and Kin2 Modulates MRNA Splicing in the Unfolded Protein Response in Yeast

Overview

Journal Sci Signal

Specialties Cell Biology
Physiology
Science

Date 2021 May 26

PMID 34035143

Citations 5

Authors

Chandrima Ghosh

Jagadeesh Kumar Uppala

Leena Sathe

Charlotte I Hammond

Ashish Anshu

P Raj Pokkuluri

Benjamin E Turk

Madhusudan Dey

Affiliations

Soon will be listed here.

Abstract

During cellular stress in the budding yeast , an endoplasmic reticulum (ER)-resident dual kinase and RNase Ire1 splices an intron from 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 mRNA processing. Here, we showed that an RNA-protein complex that included the endocytic proteins Pal1 and Pal2 mediated mRNA splicing downstream of Kin1 and Kin2. We found that Pal1 and Pal2 bound to the 3' untranslated region (3'UTR) of mRNA, and a yeast strain lacking both Pal1 and Pal2 was deficient in mRNA processing. We also showed that Kin1 and Kin2 directly phosphorylated Pal2, and that a nonphosphorylatable Pal2 mutant could not rescue the UPR defect in a Δ Δ strain. Thus, our work uncovers a Kin1/2-Pal2 signaling pathway that coordinates mRNA processing and ER homeostasis.

Citing Articles

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