PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin

Sakono, Masafumi; Seko, Akira; Takeda, Yoichi; Ito, Yukishige

doi:10.1016/j.bbrc.2014.08.041

Cited by 22 publications

(12 citation statements)

References 22 publications

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“…Mouse tau MBD fragment was prepared as described in the Supplementary Methods. Chaperones, CRT, ERp57, and PDI, were prepared according to a previous report 31 . The plant extract library and the aromatic low-molecular weight compound library were prepared as described in the Supplementary Methods.…”

Section: Methodsmentioning

confidence: 99%

An automated microliter-scale high-throughput screening system (MSHTS) for real-time monitoring of protein aggregation using quantum-dot nanoprobes

Sasaki

Tainaka

Ando

et al. 2019

Sci Rep

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Protein aggregation is the principal component of numerous protein misfolding pathologies termed proteinopathies, such as Alzheimer’s disease, Parkinson’s disease, prion disease, and AA amyloidosis with unmet treatment needs. Protein aggregation inhibitors have great potential for the prevention and treatment of proteinopathies. Here we report the development of an automated real-time microliter-scale high throughput screening (MSHTS) system for amyloid aggregation inhibitors using quantum-dot nanoprobes. Screening 504 crude extracts and 134 low molecular weight aromatic compounds revealed the relationship of amyloid-β (Aβ) aggregation inhibitory activities of plant extracts using a plant-based classification. Within the eudicots, rosids, Geraniales and Myrtales showed higher activity. Screening low molecular weight aromatic compounds demonstrated that the structure of tropolone endows it with potential Aβ aggregation inhibitory activity. The activity of the most active tropolone derivative was higher than that of rosmarinic acid. MSHTS also identified three chaperone molecules as tau aggregation inhibitors. These results demonstrate that our automated MSHTS system is a novel and robust tool that can be adapted to a wide range of compounds and aggregation-prone polypeptides.

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Section: Methodsmentioning

confidence: 99%

An automated microliter-scale high-throughput screening system (MSHTS) for real-time monitoring of protein aggregation using quantum-dot nanoprobes

Sasaki

Tainaka

Ando

et al. 2019

Sci Rep

Self Cite

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“…Whereas an association of PDI with the P-domain of CRT has originally been reported (86, 87), subsequent studies showed that this interaction requires unphysiologic calcium concentration and should, therefore, not have a physiologic relevance (83, 88, 89). In contrast, a large set of data proved a direct involvement of ERp57 in the CNX/CRT cycle (81, 82, 90–92).…”

Section: Protein Folding In the Ermentioning

confidence: 98%

N-linked sugar-regulated protein folding and quality control in the ER

Tannous

Pisoni

Hebert

et al. 2015

Seminars in Cell & Developmental Biology

212

192

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Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the lectin chaperone malectin possibly involved in a first triage of defective polypeptides. Removal of a second glucose promotes engagement of folding and quality control machineries built around the ER lectin chaperones calnexin (CNX) and calreticulin (CRT) and including oxidoreductases and peptidyl-prolyl isomerases. Deprivation of the last glucose residue dictates the release of N- glycosylated polypeptides from the lectin chaperones. Correctly folded proteins are authorized to leave the ER. Non-native polypeptides are recognized by the ER quality control key player UDP-glucose glycoprotein glucosyltransferase 1 (UGT1), re-glucosylated and re-addressed to the CNX/CRT chaperone binding cycle to provide additional opportunity for the protein to fold in the ER. Failure to attain the native structure determines the selection of the misfolded polypeptides for proteasome-mediated degradation.

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“…These lectins comprise a globular carbohydrate recognition domain (CRD) with a structural resemblance to legume lectins and an extended proline-rich segment called P-domain, which recruits ERp57, a protein disulfide isomerase (PDI) family chaperone [ 21 , 22 , 23 , 24 , 25 ], and thereby assists in the folding of the nascent glycoproteins. Beside this canonical lectin/chaperone complex, another PDI family protein, ERp29, has recently been reported to form a 1:1 complex with CRT [ 26 ]. Unlike ERp57, which possesses two catalytic thioredoxin (Trx)-like domains, ERp29 has a single Trx-like domain without the CXXC catalytic motif, indicating that this protein is not directly involved in thiol/disulfide exchange reactions.…”

Section: Glycoprotein Folding Assisted By Lectin/chaperone Complexmentioning

confidence: 99%

Emerging Structural Insights into Glycoprotein Quality Control Coupled with N-Glycan Processing in the Endoplasmic Reticulum

2015

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In the endoplasmic reticulum (ER), the sugar chain is initially introduced onto newly synthesized proteins as a triantennary tetradecasaccharide (Glc3Man9GlcNAc2). The attached oligosaccharide chain is subjected to stepwise trimming by the actions of specific glucosidases and mannosidases. In these processes, the transiently expressed N-glycans, as processing intermediates, function as signals for the determination of glycoprotein fates, i.e., folding, transport, or degradation through interactions of a series of intracellular lectins. The monoglucosylated glycoforms are hallmarks of incompletely folded states of glycoproteins in this system, whereas the outer mannose trimming leads to ER-associated glycoprotein degradation. This review outlines the recently emerging evidence regarding the molecular and structural basis of this glycoprotein quality control system, which is regulated through dynamic interplay among intracellular lectins, glycosidases, and glycosyltransferase. Structural snapshots of carbohydrate-lectin interactions have been provided at the atomic level using X-ray crystallographic analyses. Conformational ensembles of uncomplexed triantennary high-mannose-type oligosaccharides have been characterized in a quantitative manner using molecular dynamics simulation in conjunction with nuclear magnetic resonance spectroscopy. These complementary views provide new insights into glycoprotein recognition in quality control coupled with N-glycan processing.

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PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin

Cited by 22 publications

References 22 publications

An automated microliter-scale high-throughput screening system (MSHTS) for real-time monitoring of protein aggregation using quantum-dot nanoprobes

An automated microliter-scale high-throughput screening system (MSHTS) for real-time monitoring of protein aggregation using quantum-dot nanoprobes

N-linked sugar-regulated protein folding and quality control in the ER

Emerging Structural Insights into Glycoprotein Quality Control Coupled with N-Glycan Processing in the Endoplasmic Reticulum

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