PAWH1 and PAWH2 are plant-specific components of an Arabidopsis endoplasmic reticulum-associated degradation complex

Nature Communications
Liangguang LinJianming Li

Abstract

Endoplasmic reticulum-associated degradation (ERAD) is a unique mechanism to degrade misfolded proteins via complexes containing several highly-conserved ER-anchored ubiquitin ligases such as HMG-CoA reductase degradation1 (Hrd1). Arabidopsis has a similar Hrd1-containing ERAD machinery; however, our knowledge of this complex is limited. Here we report two closely-related Arabidopsis proteins, Protein Associated With Hrd1-1 (PAWH1) and PAWH2, which share a conserved domain with yeast Altered Inheritance of Mitochondria24. PAWH1 and PAWH2 localize to the ER membrane and associate with Hrd1 via EMS-mutagenized Bri1 Suppressor7 (EBS7), a plant-specific component of the Hrd1 complex. Simultaneously elimination of two PAWHs constitutively activates the unfolded protein response and compromises stress tolerance. Importantly, the pawh1 pawh2 double mutation reduces the protein abundance of EBS7 and Hrd1 and inhibits degradation of several ERAD substrates. Our study not only discovers additional plant-specific components of the Arabidopsis Hrd1 complex but also reveals a distinct mechanism for regulating the Hrd1 stability.

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Citations

Dec 16, 2019·The New Phytologist·Qian ChenQi Xie
Jul 24, 2020·International Journal of Molecular Sciences·Victor P Bulgakov, Tatiana V Avramenko
Jun 24, 2020·International Journal of Molecular Sciences·Juan Mao, Jianming Li
Nov 3, 2020·Molecular Plant·Jing-Liang SunJian-Xiang Liu
Nov 2, 2020·Journal of Experimental Botany·Ze PengJianping Wang

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Methods Mentioned

BETA
ubiquitination
protein folding
transgenic
immunoprecipitation
coimmunoprecipitation
two-hybrid
coIP
density-gradient centrifugation
ubiquitinate
PCR

Software Mentioned

Proteome Discoverer
Image Lab TM
LAS AF
MODEL
BLAST
Mascot Daemon
ImageJ
SWISS

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