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Ca2+ Regulates ERp57-Calnexin Complex Formation

Title
Ca2+ Regulates ERp57-Calnexin Complex Formation
Authors
Tanikawa, YuyaKanemura, ShingoIto, DaiLin, YuxiMatsusaki, MotonoriKuroki, KimikoYamaguchi, HiroshiMaenaka, KatsumiLee, Young-HoInaba, KenjiOkumura, Masaki
DGIST Authors
Tanikawa, Yuya; Kanemura, Shingo; Ito, Dai; Lin, Yuxi; Matsusaki, Motonori; Kuroki, Kimiko; Yamaguchi, Hiroshi; Maenaka, Katsumi; Lee, Young-Ho; Inaba, Kenji; Okumura, Masaki
Issue Date
2021-05
Citation
Molecules, 26(10), 2853
Type
Article
Author Keywords
endoplasmic reticulumoxidative foldingchaperonecalnexinERp57human leukocyte antigenCa2+
Keywords
PROTEIN-DISULFIDE-ISOMERASECLASS-IFAMILY-MEMBERSCALNEXINERP57CALCIUMBINDINGPDIOXIDOREDUCTASESCALRETICULIN
ISSN
1420-3049
Abstract
ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER). In concert with ER lectin-like chaperones calnexin and calreticulin (CNX/CRT), ERp57 functions in virtually all folding stages from co-translation to post-translation, and thus plays a critical role in maintaining protein homeostasis, with direct implication for pathology. Here, we present mechanisms by which Ca2+ regulates the formation of the ERp57-calnexin complex. Biochemical and isothermal titration calorimetry analyses revealed that ERp57 strongly interacts with CNX via a non-covalent bond in the absence of Ca2+. The ERp57-CNX complex not only promoted the oxidative folding of human leukocyte antigen heavy chains, but also inhibited client aggregation. These results suggest that this complex performs both enzymatic and chaperoning functions under abnormal physiological conditions, such as Ca2+ depletion, to effectively guide proper oxidative protein folding. The findings shed light on the molecular mechanisms underpinning crosstalk between the chaperone network and Ca2+. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
URI
http://hdl.handle.net/20.500.11750/15463
DOI
10.3390/molecules26102853
Publisher
MDPI AG
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