Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding

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dc.contributor.authorHyunjoo Cha-
dc.contributor.authorK S Sung-
dc.contributor.authorJoonsung Hwang-
dc.contributor.authorKyeong A Kim-
dc.contributor.authorJi-eun Yu-
dc.contributor.authorY D Yoo-
dc.contributor.authorJ M Jang-
dc.contributor.authorD H Han-
dc.contributor.authorM Molstad-
dc.contributor.authorJung Gi Kim-
dc.contributor.authorY J Lee-
dc.contributor.authorA Zakrzewska-
dc.contributor.authorSu Hyeon Kim-
dc.contributor.authorS T Kim-
dc.contributor.authorS Y Kim-
dc.contributor.authorHee Gu Lee-
dc.contributor.authorNak Kyun Soung-
dc.contributor.authorJong Seog Ahn-
dc.contributor.authorA Ciechanover-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorY T Kwon-
dc.date.accessioned2017-04-19T10:08:41Z-
dc.date.available2017-04-19T10:08:41Z-
dc.date.issued2015-
dc.identifier.issn1465-7392-
dc.identifier.uri10.1038/ncb3177ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12722-
dc.description.abstractWe show that ATE1-encoded Arg-transfer RNA transferase (R-transferase) of the N-end rule pathway mediates N-terminal arginylation of multiple endoplasmic reticulum (ER)-residing chaperones, leading to their cytosolic relocalization and turnover. N-terminal arginylation of BiP (also known as GRP78), protein disulphide isomerase and calreticulin is co-induced with autophagy during innate immune responses to cytosolic foreign DNA or proteasomal inhibition, associated with increased ubiquitylation. Arginylated BiP (R-BiP) is induced by and associated with cytosolic misfolded proteins destined for p62 (also known as sequestosome 1, SQSTM1) bodies. R-BiP binds the autophagic adaptor p62 through the interaction of its N-terminal arginine with the p62 ZZ domain. This allosterically induces self-oligomerization and aggregation of p62 and increases p62 interaction with LC3, leading to p62 targeting to autophagosomes and selective lysosomal co-degradation of R-BiP and p62 together with associated cargoes. In this autophagic mechanism, Nt-arginine functions as a delivery determinant, a degron and an activating ligand. Bioinformatics analysis predicts that many ER residents use arginylation to regulate non-ER processes.-
dc.publisherSpringer-Nature Pub Group-
dc.titleAmino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding-
dc.title.alternativeAmino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding-
dc.typeArticle-
dc.citation.titleNature Cell Biology-
dc.citation.number7-
dc.citation.endPage929-
dc.citation.startPage917-
dc.citation.volume17-
dc.contributor.affiliatedAuthorHyunjoo Cha-
dc.contributor.affiliatedAuthorJoonsung Hwang-
dc.contributor.affiliatedAuthorKyeong A Kim-
dc.contributor.affiliatedAuthorJi-eun Yu-
dc.contributor.affiliatedAuthorJung Gi Kim-
dc.contributor.affiliatedAuthorSu Hyeon Kim-
dc.contributor.affiliatedAuthorHee Gu Lee-
dc.contributor.affiliatedAuthorNak Kyun Soung-
dc.contributor.affiliatedAuthorJong Seog Ahn-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.alternativeName차현주-
dc.contributor.alternativeName성기사-
dc.contributor.alternativeName황준성-
dc.contributor.alternativeName김경아-
dc.contributor.alternativeName유지은-
dc.contributor.alternativeName유영동-
dc.contributor.alternativeName장준민-
dc.contributor.alternativeName한동훈-
dc.contributor.alternativeNameMolstad-
dc.contributor.alternativeName김정기-
dc.contributor.alternativeName이윤지-
dc.contributor.alternativeNameZakrzewska-
dc.contributor.alternativeName김수현-
dc.contributor.alternativeName김성태-
dc.contributor.alternativeName김선용-
dc.contributor.alternativeName이희구-
dc.contributor.alternativeName성낙균-
dc.contributor.alternativeName안종석-
dc.contributor.alternativeNameCiechanover-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeName권용태-
dc.identifier.bibliographicCitationNature Cell Biology, vol. 17, no. 7, pp. 917-929-
dc.identifier.doi10.1038/ncb3177-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Nucleic Acid Therapeutics Research Center > 1. Journal Articles
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Division of Biomedical Research > Immunotherapy Research Center > 1. Journal Articles
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