Modulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP

Autophagy

Volumn 12, Issue 2, 2016, Pages 426-428

  Cha Molstad, Hyunjoo ^a   Yu, Ji Eun ^a,b   Lee, Su Hyun ^c   Kim, Jung Gi ^a   Sung, Ki Sa ^c,d   Hwang, Joonsung ^a   Yoo, Young Dong ^a,c   Lee, Yoon Jee ^c   Kim, Sung Tae ^c,d   Lee, Dae Hee ^e   Ciechanover, Aaron ^c,f   Kim, Bo Yeon ^a   Kwon, Yong Tae ^c  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Chungbuk National University   (South Korea)

^c Seoul National University   (South Korea)

^d UNIVERSITY OF PITTSBURGH   (United States)

^e Korea University College of Medicine   (South Korea)

^f TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

ATE1 R transferase; N end rule pathway; Protein arginylation; Protein quality control; Proteolysis

Indexed keywords

CHAPERONE; PROTEIN P62; UBIQUITIN; ARGININE; HEAT SHOCK PROTEIN; MOLECULAR CHAPERONE GRP78; PROTEASOME; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

ARGINYLATION; ARTICLE; AUTOPHAGOSOME; CHEMICAL REACTION; ENDOPLASMIC RETICULUM; NONHUMAN; POLYMERIZATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; ANIMAL; BIOLOGICAL MODEL; HUMAN; METABOLISM;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; ARGININE; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HUMANS; MODELS, BIOLOGICAL; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOLYSIS; UBIQUITIN;

EID: 84964483788     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2015.1126047     Document Type: Article

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