Glycan dependent refolding activity of ER glucosyltransferase (UGGT)

Wang, Ning; Seko, Akira; Takeda, Yoichi; Ito, Yukishige

doi:10.1016/j.bbagen.2020.129709

Cited by 12 publications

(8 citation statements)

References 49 publications

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“…Glycoproteins that have failed to attain correct folding within a certain timeframe are degraded via ER‐associated degradation. In addition, we showed that UGGT1 facilitates the folding of denatured glycoproteins in vitro , suggesting that it might secondarily be a bona fide chaperone in the ER [15] …”

Section: Introductionmentioning

confidence: 92%

“…In addition, we showed that UGGT1 facilitates the folding of denatured glycoproteins in vitro, suggesting that it might secondarily be a bona fide chaperone in the ER. [15] Selenoprotein F (SelenoF), which forms a heterodimer with UGGT1 and UGGT2, is deemed to act as a disulfide isomerase because the redox potential of Drosophila melanogaster SelenoF (DmSelenoF) is within the range of that of oxidoreductases involved in cysteine thiol-disulfide exchange. [16] A TRX-like domain of human SelenoF containing Sec was recently synthesized and exhibited a redox potential of approximately À 256 mV, although this partial structure did not affect the folding of two model proteins (bovine pancreatic trypsin inhibitor and hirudin).…”

Section: Introductionmentioning

confidence: 99%

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Analysis of Selenoprotein F Binding to UDP‐Glucose:Glycoprotein Glucosyltransferase (UGGT) by a Photoreactive Crosslinker

et al. 2022

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In the endoplasmic reticulum glycoprotein quality control system, UDP-glucose : glycoprotein glucosyltransferase (UGGT) functions as a folding sensor. Although it is known to form a heterodimer with selenoprotein F (SelenoF), the details of the complex formation remain obscure. A pulldown assay using cotransfected SelenoF and truncated mutants of human UGGT1 (HUGT1) revealed that SelenoF binds to the TRXL2 domain of HUGT1. Additionally, a newly developed photoaffinity crosslinker was selectively introduced into cysteine residues of recombinant SelenoF to determine the spatial orientation of SelenoF to HUGT1. The crosslinking experiments showed that SelenoF formed a covalent bond with amino acids in the TRXL3 region and the interdomain between βS2 and GT24 of HUGT1 via the synthetic crosslinker. SelenoF might play a role in assessing and refining the disulfide bonds of misfolded glycoproteins in the hydrophobic cavity of HUGT1 as it binds to the highly flexible region of HUGT1 to reach its long hydrophobic cavity. Clarification of the SelenoF-binding domain of UGGT and its relative position will help predict and reveal the function of SelenoF from a structural perspective.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Analysis of Selenoprotein F Binding to UDP‐Glucose:Glycoprotein Glucosyltransferase (UGGT) by a Photoreactive Crosslinker

et al. 2022

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“…Especially,e gg yolk is ar ich source of complex-type [34] as well as high-mannose-type glycans, [35] from which M9 and G1M9 were isolatedi nA snlinked forms.T hey have been utilized extensively as components for chemical synthesis of glycoproteins. [36] M9-Asn was used as as tartingm aterialf or chemoenzymatic synthesis of glycosylated RNase [37] by endoglycosidase catalyzed transglycosylation. [38]…”

Section: Synthesis Of High-mannose-type Glycansmentioning

confidence: 99%

Chemical‐Synthesis‐Based Approach to Glycoprotein Functions in the Endoplasmic Reticulum

Ito

Kajihara

Takeda

2020

Chemistry A European J

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The introduction of Asn‐linked glycans to nascent polypeptides occurs in the lumen of the endoplasmic reticulum of eukaryotic cells. After the removal of specific sugar residues, glycoproteins acquire signals in the glycoprotein quality control (GPQC) system and enter the folding cycle composed of lectin‐chaperones calnexin (CNX) and calreticulin (CRT), glucosidase II (G‐II), and UDP‐Glc:glycoprotein glucosyltransferase (UGGT). G‐II initiates glycoproteins’ entry and exit from the cycle, and UGGT serves as the “folding sensor”. This account summarizes our effort to analyze the properties of enzymes and lectins that play important roles in GPQC, especially those involved in the CNX/CRT cycle. To commence our study, general methods for the synthesis of high‐mannose‐type glycans and glycoproteins were established. Based on these, various substrates to analyze components of the GPQC were created, and properties of CRT, G‐II, and UGGT have been clarified.

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“…Apart from TRXL2, other untested UGGT regions potentially harboring exposed hydrophobic patches are the CtUGGT TRXL4 disordered region (CtUGGT 243-285), the flexible linker around the endo-proteolysis site between the bS2 and GT24 domains (CtUGGT 1,195), and the residues between the last helix and the ER retrieval motif at the C terminus (CtUGGT 1,474-1,510) (Roversi et al, 2017). Experiments described in a recent report ascribe intrinsic refoldase activity to UGGT (Wang et al, 2020) and await being reproduced. Again, structural and functional data from a range of UGGT mutants and glycoprotein substrates will be required to further test these hypotheses and fully dissect the UGGT structure-function relationship.…”

Section: Articlementioning

confidence: 99%

Clamping, Bending, and Twisting Inter-Domain Motions in the Misfold-Recognising Portion of UDP-Glucose: Glycoprotein Glucosyl-Transferase

et al. 2020

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Glycan dependent refolding activity of ER glucosyltransferase (UGGT)

Cited by 12 publications

References 49 publications

Analysis of Selenoprotein F Binding to UDP‐Glucose:Glycoprotein Glucosyltransferase (UGGT) by a Photoreactive Crosslinker

Analysis of Selenoprotein F Binding to UDP‐Glucose:Glycoprotein Glucosyltransferase (UGGT) by a Photoreactive Crosslinker

Chemical‐Synthesis‐Based Approach to Glycoprotein Functions in the Endoplasmic Reticulum

Clamping, Bending, and Twisting Inter-Domain Motions in the Misfold-Recognising Portion of UDP-Glucose: Glycoprotein Glucosyl-Transferase

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