ArticleThe Journal of biological chemistry2011
Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- The Interaction BetweenPathogens (Basel, Switzerland) · 2026Article
- Molecular and Functional Analysis of Calcium Binding by a Cancer-linked Calreticulin Mutant.bioRxiv : the preprint server for biology · 2025Article
- Challenges in the Evolving Role of Calreticulin as a Promising Target for Precision Medicine in Myeloproliferative Neoplasms.Cancers · 2025Review
- Conformational ligand-directed targeting of calcium-dependent receptors in acute trauma.Med (New York, N.Y.) · 2025Article
- Effects of Calreticulin Mutations on HLA Class I Expression in Myeloproliferative Neoplasms.bioRxiv : the preprint server for biology · 2025Article
- Calreticulin-From the Endoplasmic Reticulum to the Plasma Membrane-Adventures of a Wandering Protein.Cancers · 2025Review
- Review
- Effects of calreticulin mutations on cell transformation and immunity.Journal of cellular and molecular medicine · 2023Review
- Structural and Dynamic Differences between Calreticulin Mutants Associated with Essential Thrombocythemia.Biomolecules · 2023Article
- Expression properties, structural features and functional analysis of CALR E381A in MPN patients.American journal of translational research · 2023Article
- The cellular response to ocean warming inFrontiers in microbiology · 2023Article
- The many faces of parasite calreticulin.Frontiers in immunology · 2023Review
- Roles of Calreticulin in Protein Folding, Immunity, Calcium Signaling and Cell Transformation.Progress in molecular and subcellular biology · 2021Article
- Calreticulin enhances the secretory trafficking of a misfolded α-1-antitrypsin.The Journal of biological chemistry · 2020Article
- Calnexin cycle - structural features of the ER chaperone system.The FEBS journal · 2020Review
- The Endoplasmic Reticulum and Calcium Homeostasis in Pancreatic Beta Cells.Endocrinology · 2020Review
- Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.Biomolecules · 2018Review
- Dissecting physical structure of calreticulin, an intrinsically disordered CaJournal of biomolecular structure & dynamics · 2018Article
- The Calreticulin control of human stress erythropoiesis is impaired by JAK2V617F in polycythemia vera.Experimental hematology · 2017Article
- Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function.Frontiers in cell and developmental biology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Calreticulin is a soluble calcium-binding chaperone of the endoplasmic reticulum (ER) that is also detected on the cell surface and in the cytosol. Calreticulin contains a single high affinity calcium-binding site within a globular domain and multiple low affinity sites within a C-terminal acidic region. We show that the secondary structure of calreticulin is remarkably thermostable at a given calcium concentration. Rather than corresponding to complete unfolding events, heat-induced structural transitions observed for calreticulin relate to tertiary structural changes that expose hydrophobic residues and reduce protein rigidity. The thermostability and the overall secondary structure content of calreticulin are impacted by the divalent cation environment, with the ER range of calcium concentrations enhancing stability, and calcium-depleting or high calcium environments reducing stability. Furthermore, magnesium competes with calcium for binding to calreticulin and reduces thermostability. The acidic domain of calreticulin is an important mediator of calcium-dependent changes in secondary structure content and thermostability. Together, these studies indicate interactions between the globular and acidic domains of calreticulin that are impacted by divalent cations. These interactions influence the structure and stability of calreticulin, and are likely to determine the multiple functional activities of calreticulin in different subcellular environments.
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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.