ArticleThe Journal of biological chemistry2011
Structural and functional relationships between the lectin and arm domains of calreticulin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 53 citations in OpenAlex.
- Calcium-mediated calreticulin-IRE1α interaction drives dynamic fluctuation of IRE1α activity under chronic endoplasmic reticulum stress.Nature communications · 2026Article
- Crystal structure ofFrontiers in immunology · 2024Article
- Z-αScience advances · 2022Article
- Zinc-dependent multimerization of mutant calreticulin is required for MPL binding and MPN pathogenesis.Blood advances · 2021Article
- Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease.Progress in molecular and subcellular biology · 2021Article
- Roles of Calreticulin in Protein Folding, Immunity, Calcium Signaling and Cell Transformation.Progress in molecular and subcellular biology · 2021Article
- Structural Analysis of Calreticulin, an Endoplasmic Reticulum-Resident Molecular Chaperone.Progress in molecular and subcellular biology · 2021Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
- Tumor-associated calreticulin variants functionally compromise the peptide loading complex and impair its recruitment of MHC-I.The Journal of biological chemistry · 2018Article
- Article
- Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.The Journal of biological chemistry · 2016Article
- Clinical Manifestation of Calreticulin Gene Mutations in Essential Thrombocythemia without Janus Kinase 2 and MPL Mutations: A Chinese Cohort Clinical Study.Chinese medical journal · 2016Article
- The C-Terminal Acidic Region of Calreticulin Mediates Phosphatidylserine Binding and Apoptotic Cell Phagocytosis.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Glycoprotein folding and quality-control mechanisms in protein-folding diseases.Disease models & mechanisms · 2014Review
- Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2.The New England journal of medicine · 2013Article
- Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.The Journal of biological chemistry · 2013Article
- Calreticulin in the immune system: ins and outs.Trends in immunology · 2013Review
- Protein secretion and the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2012Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Calreticulin and calnexin are key components in maintaining the quality control of glycoprotein folding within the endoplasmic reticulum. Although their lectin function of binding monoglucosylated sugar moieties of glycoproteins is well documented, their chaperone activity in suppressing protein aggregation is less well understood. Here, we use a series of deletion mutants of calreticulin to demonstrate that its aggregation suppression function resides primarily within its lectin domain. Using hydrophobic peptides as substrate mimetics, we show that aggregation suppression is mediated through a single polypeptide binding site that exhibits a K(d) for peptides of 0.5-1 μM. This site is distinct from the oligosaccharide binding site and differs from previously identified sites of binding to thrombospondin and GABARAP (4-aminobutyrate type A receptor-associated protein). Although the arm domain of calreticulin was incapable of suppressing aggregation or binding hydrophobic peptides on its own, it did contribute to aggregation suppression in the context of the whole molecule. The high resolution x-ray crystal structure of calreticulin with a partially truncated arm domain reveals a marked difference in the relative orientations of the arm and lectin domains when compared with calnexin. Furthermore, a hydrophobic patch was detected on the arm domain that mediates crystal packing and may contribute to calreticulin chaperone function.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.