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MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana

Authors
 Jong Hum Kim,a,1 Seok Keun Cho,a,1 Tae Rin Oh,a Moon Young Ryu,a Seong Wook Yang,a,b,2 and Woo Taek Kima,2 
Citation
 Proceedings of the National Academy of Sciences of the United States of America, Vol.114(46) : E10009-E10017, 2017 
Journal Title
 Proceedings of the National Academy of Sciences of the United States of America 
ISSN
 0027-8424 
Issue Date
2017
MeSH
Arabidopsis/genetics ; Arabidopsis/growth & development ; Arabidopsis/metabolism* ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism* ; Cytoplasm/metabolism ; DNA, Plant ; Gene Expression Regulation, Plant ; Genes, Plant/genetics ; Phenotype ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding* ; Protein Interaction Domains and Motifs ; Proteolysis ; Proteostasis* ; Recombinant Proteins ; Sequence Analysis ; Sequence Analysis, RNA ; Stress, Psychological ; Two-Hybrid System Techniques ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism* ; Ubiquitins/metabolism ; Yeasts/genetics
Keywords
E3 ligase ; PQC ; proteostasis
Abstract
Ubiquitin E3 ligases are crucial for eliminating misfolded proteins before they form cytotoxic aggregates that threaten cell fitness and survival. However, it remains unclear how emerging misfolded proteins in the cytoplasm can be selectively recognized and eliminated by E3 ligases in plants. We found that Misfolded Protein Sensing RING E3 ligase 1 (MPSR1) is an indispensable E3 ligase required for plant survival after protein-damaging stress. Under no stress, MPSR1 is prone to rapid degradation by the 26S proteasome, concealing its protein quality control (PQC) E3 ligase activity. Upon proteotoxic stress, MPSR1 directly senses incipient misfolded proteins and tethers ubiquitins for subsequent degradation. Furthermore, MPSR1 sustains the structural integrity of the proteasome complex at the initial stage of proteotoxic stress. Here, we suggest that the MPSR1 pathway is a constitutive mechanism for proteostasis under protein-damaging stress, as a front-line surveillance system in the cytoplasm.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/161501
DOI
10.1073/pnas.1713574114
Appears in Collections:
1. Journal Papers (연구논문) > 1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실)
Yonsei Authors
유문영(Ryu, Moon Young)
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