ReviewProtein science : a publication of the Protein Society1996
The C2 domain calcium-binding motif: structural and functional diversity.
Review in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 301 papers.
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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
301 citing papers in PubMed, 816 citations in OpenAlex.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The multifaceted significance of phosphoinositides in endocytic trafficking.FEBS letters · 2026Review
- Novel gain-of-function mutation in dysferlin causes vesicle trafficking defect and IL-1 mediated autoinflammation.medRxiv : the preprint server for health sciences · 2026Article
- Electrostatics and Local Aromatic Residues Govern Lipid Binding and Membrane Penetration of Synaptotagmin C2 Domains.bioRxiv : the preprint server for biology · 2026Article
- Structural characterization of the human CC2D1A fragment associated with non-syndromic intellectual disability (NSID).Bioscience reports · 2026Article
- Identification and validation of an interaction between the E3 ubiquitin ligase WWP1 and the Transcriptional Co-Activator WBP2 in the human heart.Biology open · 2026Article
- Interactome Analysis of the CC2D1A Scaffold Reveals Novel Neuronal Interactions and a Postsynaptic Role.Molecular & cellular proteomics : MCP · 2026Article
- Structure and dynamics of a multidomain nitric oxide synthase regulated by a C2 domain.Science advances · 2026Article
- Genome-Wide Identification of theInternational journal of molecular sciences · 2026Article
- A Trichomonas vaginalis C2-XYPPX-repeat protein with a structured C2 domain displaying dampened flexibility upon binding calcium.Biochimie · 2026Article
- Identification of theFrontiers in plant science · 2026Article
- Integrated genomic and transcriptomic analysis of maize SRC2-like genes highlights divergent roles in abiotic stress responses.Frontiers in plant science · 2026Article
- Article
- Connecting cilium, stress response, and proteostasis abnormalities inform variant and therapy assessment in RPGRIP1 retinal organoids.Stem cell reports · 2025Article
- Article
- Grapevine protein Src2 mediates plant disease resistance during Lasiodiplodia theobromae infection.Plant physiology · 2025Article
- Targeting MET Signalling Activated by CPNE3-RACK1 Interaction Through VWFA Domain to Suppress Lung Cancer Progression.Journal of cellular and molecular medicine · 2025Article
- Crustacean Protein Kinases A and C: Bioinformatic Characterization in Decapods and Other Non-Model Organisms.International journal of molecular sciences · 2025Article
- SH2-mediated steric occlusion of the C2 domain regulates autoinhibition of SHIP1 inositol 5-phosphatase.bioRxiv : the preprint server for biology · 2025Article
- The Multifaceted Role of Calcium Signaling in Regulated Necrosis.Biomolecules · 2025Review
241 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The C2 domain is a Ca(2+)-binding motif of approximately 130 residues in length originally identified in the Ca(2+)-dependent isoforms of protein kinase C. Single and multiple copies of C2 domains have been identified in a growing number of eukaryotic signalling proteins that interact with cellular membranes and mediate a broad array of critical intracellular processes, including membrane trafficking, the generation of lipid-second messengers, activation of GTPases, and the control of protein phosphorylation. As a group, C2 domains display the remarkable property of binding a variety of different ligands and substrates, including Ca2+, phospholipids, inositol polyphosphates, and intracellular proteins. Expanding this functional diversity is the fact that not all proteins containing C2 domains are regulated by Ca2+, suggesting that some C2 domains may play a purely structural role or may have lost the ability to bind Ca2+. The present review summarizes the information currently available regarding the structure and function of the C2 domain and provides a novel sequence alignment of 65 C2 domain primary structures. This alignment predicts that C2 domains form two distinct topological folds, illustrated by the recent crystal structures of C2 domains from synaptotagmin 1 and phosphoinositide-specific phospholipase C-delta 1, respectively. The alignment highlights residues that may be critical to the C2 domain fold or required for Ca2+ binding and regulation.
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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.