FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis | Zendy

Xi Chen | Zendy; Lang-Huan Duan | Zendy; Pengcheng Luo | Zendy; Gang Hu | Zendy; Xin Yu | Zendy; Jie Liu | Zendy; Lu Han | Zendy; Bin Liu | Zendy

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FBXO6-Mediated Ubiquitination and Degradation of Ero1L Inhibits Endoplasmic Reticulum Stress-Induced Apoptosis

Author(s) -

Xi Chen,

Lang-Huan Duan,

Pengcheng Luo,

Gang Hu,

Xin Yu,

Jie Liu,

Lu Han,

Bin Liu

Publication year - 2016

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000452517

Subject(s) - endoplasmic reticulum , ubiquitin , ubiquitin ligase , unfolded protein response , endoplasmic reticulum associated protein degradation , microbiology and biotechnology , chemistry , protein disulfide isomerase , glycoprotein , biology , biochemistry , gene

FBXO6 is the substrate recognition component of a Skp1-Cullin1-F-box protein (SCF) ubiquitin E3 ligase complex, recognizing the chitobiose in unfolded N-glycoprotein to target glycoproteins for polyubiquitination and degradation. Although how FBXO6 recognizes glycoprotein has been fully investigated, the ubiquitination substrates of FBXO6 remain largely unknown. Previously, we have systematically identified the glycoproteins that interact with FBXO6 in an N-glycan dependent manner by LC/MS spectrum and confirmed the interaction between FBXO6 and glycosylated Ero1L, a protein disulfide oxidase in endoplasmic reticulum (ER).

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