Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface

Serve, Olivier; Kamiya, Yukiko; Maeno, Aya; Nakano, Michiko; Murakami, Chiho; Sasakawa, Hiroaki; Yamaguchi, Yoshiki; Harada, T.; Kurimoto, Eiji; Yagi-Utsumi, Maho; Iguchi, Takeshi; Inaba, Kenji; Kikuchi, Jun; Asami, Osamu; Kajino, Toshitaka; Oka, Toshihiko; Nakasako, Masayoshi; Kato, Koichi

doi:10.1016/j.jmb.2009.11.049

Cited by 58 publications

(78 citation statements)

References 47 publications

(54 reference statements)

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“…As a consequence, the affinity for ERO1␣ is more than 10-fold lower for oxidized than for reduced PDI. Recent analyses revealed that oxidation of the active site of the PDI aЈ-domain induced the spatial rearrangement of the bЈ-and aЈ-domains through the conformational change of the x-linker region, leading to enhanced exposure of the substrate-binding hydrophobic surface and significant changes in the solvation pattern (51,52). Consistently, the mobile x-linker region (53,54) could regulate substrate binding.…”

Section: Discussionmentioning

confidence: 98%

Molecular Bases of Cyclic and Specific Disulfide Interchange between Human ERO1α Protein and Protein-disulfide Isomerase (PDI)

Masui

Vavassori

Fagioli

et al. 2011

Journal of Biological Chemistry

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In the endoplasmic reticulum (ER) of human cells, ERO1␣ and protein-disulfide isomerase (PDI) constitute one of the major electron flow pathways that catalyze oxidative folding of secretory proteins. Specific and limited PDI oxidation by ERO1␣ is essential to avoid ER hyperoxidation. To investigate how ERO1␣ oxidizes PDI selectively among more than 20 ERresident PDI family member proteins, we performed docking simulations and systematic biochemical analyses. Our findings reveal that a protruding ␤-hairpin of ERO1␣ specifically interacts with the hydrophobic pocket present in the redox-inactive PDI b-domain through the stacks between their aromatic residues, leading to preferred oxidation of the C-terminal PDI a-domain. ERO1␣ associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1␣ to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket. The interaction of ERO1␣ with ERp44, another PDI family member protein, was also analyzed. Notably, ERO1␣-dependent PDI oxidation was inhibited by a hyperactive ERp44 mutant that lacks the C-terminal tail concealing the substrate-binding hydrophobic regions. The potential ability of ERp44 to inhibit ERO1␣ activity may suggest its physiological role in ER redox and protein homeostasis.

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Section: Discussionmentioning

confidence: 98%

Molecular Bases of Cyclic and Specific Disulfide Interchange between Human ERO1α Protein and Protein-disulfide Isomerase (PDI)

Masui

Vavassori

Fagioli

et al. 2011

Journal of Biological Chemistry

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“…In human PDI, the a9 domain was first oxidized by Ero1-a, which then oxidizes the a domain, and the reduced a9 domain is oxidized by Ero1-a. During the sequential transfer of disulfide bonds, PDI dynamically changes its structure from a closed form to an open form (Nakasako et al, 2010;Serve et al, 2010;Wang et al, 2013). Subsequently, disulfide bonds are transferred from the GmPDIM to either the a or a9 domain of GmPDIL-2 (3) and from the oxidized GmPDIL-2 to a protein substrate (4).…”

Section: Discussionmentioning

confidence: 99%

Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and ERO1 in Soybean

et al. 2015

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“…The final concentration of ANS was 140 M. An RNase A solution (0.1 mg/ml) was used as a control. The hydrophobicity of ribophorin I was monitored by measuring tryptophan fluorescence as described previously (22).…”

Section: Protein Identification By Maldi-tof Ms-coomassiementioning

confidence: 99%

Malectin Forms a Complex with Ribophorin I for Enhanced Association with Misfolded Glycoproteins

Qin

Matsumoto

et al. 2012

Journal of Biological Chemistry

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Background: Malectin may play a role in the quality control of glycoproteins, but the underlying molecular mechanism(s) is not known. Results: Malectin forms a complex with ribophorin I for enhanced association with misfolded glycoproteins. Conclusion: Malectin functions by forming a complex with ribophorin I. Significance: This might be the first evidence for the preferential association of malectin with misfolded glycoproteins.

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Redox-Dependent Domain Rearrangement of Protein Disulfide Isomerase Coupled with Exposure of Its Substrate-Binding Hydrophobic Surface

Cited by 58 publications

References 47 publications

Molecular Bases of Cyclic and Specific Disulfide Interchange between Human ERO1α Protein and Protein-disulfide Isomerase (PDI)

Molecular Bases of Cyclic and Specific Disulfide Interchange between Human ERO1α Protein and Protein-disulfide Isomerase (PDI)

Cooperative Protein Folding by Two Protein Thiol Disulfide Oxidoreductases and ERO1 in Soybean

Malectin Forms a Complex with Ribophorin I for Enhanced Association with Misfolded Glycoproteins

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