Analysis of the specific interactions between the lectin domain of malectin and diglucosides

Schallus, Thomas; Fehér, Krisztina; Sternberg, Ulrich; Rybin, Vladimir; Muhle‐Goll, Claudia

doi:10.1093/glycob/cwq059

Cited by 63 publications

(64 citation statements)

References 47 publications

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“…Malectin is an ER-localized lectin expressed by metazoan organisms that binds the terminal Glc α,1–3 Glc disaccharide in the GN 2 M 9 G 2 trimming intermediate of protein bound glycans [16,17]. The role of malectin in ER homeostasis is not well understood, in part because the recognition determinant (Glc α,1–3 Glc disaccharide) for malectin is a transient trimming intermediate that precedes formation of the monoglucosylated glycan that is recognized by calnexin and calreticulin [1].…”

Section: Metazoan Cells Express Two Oligosaccharyltransferase Complexesmentioning

confidence: 99%

N-linked glycosylation and homeostasis of the endoplasmic reticulum

Cherepanova

Shrimal

Gilmore

2016

Current Opinion in Cell Biology

214

228

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Summary As a major site of protein biosynthesis, homeostasis of the endoplasmic reticulum is critical for cell viability. Asparagine linked glycosylation of newly synthesized proteins by the oligosaccharyltransferase plays a central role in ER homeostasis due to the use of protein-linked oligosaccharides as recognition and timing markers for glycoprotein quality control pathways that discriminate between correctly folded proteins and terminally malfolded proteins destined for ER associated degradation. Recent findings indicate how the oligosaccharyltransferase achieves efficient and accurate glycosylation of the diverse proteins that enter the endoplasmic reticulum. In metazoan organisms two distinct OST complexes cooperate to maximize the glycosylation of nascent proteins. The STT3B complex glycosylates acceptor sites that have been skipped by the translocation channel associated STT3A complex.

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Section: Metazoan Cells Express Two Oligosaccharyltransferase Complexesmentioning

confidence: 99%

N-linked glycosylation and homeostasis of the endoplasmic reticulum

Cherepanova

Shrimal

Gilmore

2016

Current Opinion in Cell Biology

214

228

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“…The discovery of malectin, a membrane-bound ER-resident lectin specifically binding di-glucosylated glycans, changed this view (23). Malectin is induced under conditions of ER stress (24) and is proposed to preferentially associate with off-pathway non-native conformers of well- studied glycoproteins like influenza hemagglutinin (HA) and null Hong Kong (NHK), a folding-defective variant of the secretory protein α-1-antitrypsin (α1AT).…”

Section: Protein Folding In the Ermentioning

confidence: 99%

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

Tannous

Pisoni

Hebert

et al. 2015

Seminars in Cell & Developmental Biology

215

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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“…A group of RLKs, Catharanthus roseus RLK1-like kinases (CrRLK1Ls), are of particular interest. They contain a cytoplasmic serine/threonine kinase domain and an extracellular malectin-like domain that may bind to carbohydrates, as occurs in their animal counterparts (Schallus et al, 2010;Boisson-Dernier et al, 2011). The plasma membrane localization of CrRLKs has been confirmed for at least some of the members and may require the help of cell wall-localized glycoproteins, such as glycosylphosphatidylinositol-anchored proteins .…”

Section: Signaling Mechanisms At the Cellular Scale Utilize Mechanicamentioning

confidence: 99%

Growing Out of Stress: The Role of Cell- and Organ-Scale Growth Control in Plant Water-Stress Responses

et al. 2016

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Water is the most limiting resource on land for plant growth, and its uptake by plants is affected by many abiotic stresses, such as salinity, cold, heat, and drought. While much research has focused on exploring the molecular mechanisms underlying the cellular signaling events governing water-stress responses, it is also important to consider the role organismal structure plays as a context for such responses. The regulation of growth in plants occurs at two spatial scales: the cell and the organ. In this review, we focus on how the regulation of growth at these different spatial scales enables plants to acclimate to water-deficit stress. The cell wall is discussed with respect to how the physical properties of this structure affect water loss and how regulatory mechanisms that affect wall extensibility maintain growth under water deficit. At a higher spatial scale, the architecture of the root system represents a highly dynamic physical network that facilitates access of the plant to a heterogeneous distribution of water in soil. We discuss the role differential growth plays in shaping the structure of this system and the physiological implications of such changes.

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Analysis of the specific interactions between the lectin domain of malectin and diglucosides

Cited by 63 publications

References 47 publications

N-linked glycosylation and homeostasis of the endoplasmic reticulum

N-linked glycosylation and homeostasis of the endoplasmic reticulum

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

Growing Out of Stress: The Role of Cell- and Organ-Scale Growth Control in Plant Water-Stress Responses

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