Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control

Satoh, Tadashi; Toshimori, T.; Noda, Masanori; Uchiyama, Susumu; Kato, Koichi

doi:10.1002/pro.3031

Cited by 15 publications

(15 citation statements)

References 45 publications

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“…PRKCSH consists of multiple domains, including a signal sequence for translocation across the ER membrane, an N-terminal GIIα-binding (G2B) domain, a putative coiled-coil segment, a glutamic acid and proline-rich (E/P) segment, and a C-terminal mannose 6-phosphate receptor homology (MRH) domain followed by an HDEL signal sequence for ER retention 27,28 . ER-translocation of PRKCSH is required for the expression and retention of GIIα in the ER lumen and maintaining optimal GII activity 29 . Genetic loss of PRKCSH is involved in autosomal dominant polycystic liver disease (ADPLD) 30,31 .…”

Section: Introductionmentioning

confidence: 99%

PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway

et al. 2019

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Unfolded protein response (UPR) is an adaptive mechanism that aims at restoring ER homeostasis under severe environmental stress. Malignant cells are resistant to environmental stress, which is largely due to an activated UPR. However, the molecular mechanisms by which different UPR branches are selectively controlled in tumor cells are not clearly understood. Here, we provide evidence that PRKCSH, previously known as glucosidase II beta subunit, functions as a regulator for selective activation of the IRE1α branch of UPR. PRKCSH boosts ER stress–mediated autophosphorylation and oligomerization of IRE1α through mutual interaction. PRKCSH contributes to the induction of tumor-promoting factors and to tumor resistance to ER stress. Increased levels of PRKCSH in various tumor tissues are positively correlated with the expression of XBP1-target genes. Taken together, our data provide a molecular rationale for selective activation of the IRE1α branch in tumors and adaptation of tumor cells to severe environmental stress.

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Section: Introductionmentioning

confidence: 99%

PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway

et al. 2019

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“…On the other hand, we found that residues in the distal C‐terminal region of GIIα intensively suffer from positive selection. GIIα is the only GH31 enzyme that can form a heterodimeric structure through its distal C‐terminal domain (Satoh, Toshimori, Noda, et al., ). Our finding implies that positive selection in the distal C‐terminal domain probably affects the heterodimeric structure of GIIα and folding conformation of the enzymic complexes.…”

Section: Discussionmentioning

confidence: 99%

“…GIIb can be recruited to modulate the catalytic activity and folding of GIIa and stabilizing the GII complex in vivo. Moreover, GIIb can recognize and bind cooperative substrates through its MRH domain to ensure the efficient glucose trimming of N-glycans (Deprez, Gautschi, & Helenius, 2005;Satoh, Toshimori, Noda, Uchiyama, & Kato, 2016).…”

Section: Introductionmentioning

confidence: 99%

Expression plasticity and evolutionary changes extensively shape the sugar‐mimic alkaloid adaptation of nondigestive glucosidase in lepidopteran mulberry‐specialist insects

Shi

Dai

et al. 2018

Molecular Ecology

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During the co-evolutionary arms race between plants and herbivores, insects evolved systematic adaptive plasticity to minimize the chemical defence effects of their host plants. Previous studies mainly focused on the expressional plasticity of enzymes in detoxification and digestion. However, the expressional response and adaptive evolution of other fundamental regulators against host phytochemicals are largely unknown. Glucosidase II (GII), which is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit, is an evolutionarily conserved enzyme that regulates glycoprotein folding. In this study, we found that GIIα expression of the mulberry-specialist insect was significantly induced by mulberry leaf extract, 1-deoxynojirimycin (1-DNJ), whereas GIIβ transcripts were not significantly changed. Moreover, positive selection was detected in GIIα when the mulberry-specialist insects diverged from the lepidopteran order, whereas GIIβ was mainly subjected to purifying selection, thus indicating an asymmetrically selective pressure of GII subunits. In addition, positively selected sites were enriched in the GIIα of mulberry-specialist insects and located around the 1-DNJ-binding sites and in the C-terminal region, which could result in conformational changes that affect catalytic activity and substrate-binding efficiency. These results show that expression plasticity and evolutionary changes extensively shape sugar-mimic alkaloids adaptation of nondigestive glucosidase in lepidopteran mulberry-specialist insects. Our study provides novel insights into a deep understanding of the sequestration and adaptation of phytophagous specialists to host defensive compounds.

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“…MOGS (also known as glucosidase I) is expressed in the endoplasmic reticulum and is involved in trimming N-glycans; it was the first enzyme to be identified in the pathway for processing N-linked oligosaccharides [ 30 ]. GII alpha belongs to glycoside hydrolase family 31 (GH31), which has similar functions as MOGS and is involved in trimming N-glycans [ 31 ]. As a recognized inhibitor of α-glucosidase, DNJ also inhibits MOGS and GII alpha activities [ 32 – 34 ].…”

Section: Discussionmentioning

confidence: 99%

Comparative transcriptome analysis reveals significant metabolic alterations in eri-silkworm (Samia cynthia ricini) haemolymph in response to 1-deoxynojirimycin

Zhang

Deng

et al. 2018

PLoS ONE

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Samia cynthia ricini (Lepidoptera: Saturniidae) is an important commercial silk-producing insect; however, in contrast to the silkworm, mulberry leaves are toxic to this insect because the leaves contain the component 1-deoxynojirimycin (DNJ). A transcriptomic analysis of eri-silkworm haemolymph was conducted to examine the genes related to different metabolic pathways and to elucidate the molecular mechanism underlying eri-silkworm haemolymph responses to DNJ. Eight hundred sixty-five differentially expressed genes (DEGs) were identified, among which 577 DEGs were up-regulated and 288 DEGs were down-regulated in the 2% DNJ group compared to control (ddH2O) after 12h. Based on the results of the functional analysis, these DEGs were associated with ribosomes, glycolysis, N-glycan biosynthesis, and oxidative phosphorylation. In particular, according to the KEGG analysis, 138 DEGs were involved in energy metabolism, glycometabolism and lipid metabolism, and the changes in the expression of nine DEGs were confirmed by reverse transcription quantitative PCR (RT-qPCR). Thus, DNJ induced significant metabolic alterations in eri-silkworm haemolymph. These results will lay the foundation for research into the toxic effects of DNJ on eri-silkworm as a model and provide a reference for the exploitation of new drugs in humans.

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Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control

Cited by 15 publications

References 45 publications

PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway

PRKCSH contributes to tumorigenesis by selective boosting of IRE1 signaling pathway

Expression plasticity and evolutionary changes extensively shape the sugar‐mimic alkaloid adaptation of nondigestive glucosidase in lepidopteran mulberry‐specialist insects

Comparative transcriptome analysis reveals significant metabolic alterations in eri-silkworm (Samia cynthia ricini) haemolymph in response to 1-deoxynojirimycin

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