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

Liangguang Lin, Congcong Zhang, Yongwu Chen, Yi Wang, Dinghe Wang, Xiaolei Liu, Muyang Wang, Juan Mao, Jianjun Zhang, Weiman Xing, Linchuan Liu () and Jianming Li ()
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Liangguang Lin: Chinese Academy of Sciences
Congcong Zhang: Chinese Academy of Sciences
Yongwu Chen: Chinese Academy of Sciences
Yi Wang: Chinese Academy of Sciences
Dinghe Wang: Chinese Academy of Sciences
Xiaolei Liu: Chinese Academy of Sciences
Muyang Wang: Shanghai Institute of Plant Physiology and Ecology, The Center of Excellence for Molecular Plant Sciences, Chinese Academy of Sciences
Juan Mao: South China Agricultural University
Jianjun Zhang: South China Agricultural University
Weiman Xing: Chinese Academy of Sciences
Linchuan Liu: South China Agricultural University
Jianming Li: South China Agricultural University

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-11480-7

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