ArticleThe Journal of biological chemistry2009
Structural insights into Ca2+-dependent regulation of inositol 1,4,5-trisphosphate receptors by CaBP1.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Molecular basis for a CaThe Journal of biological chemistry · 2026Article
- Structural Insights into L-Type Voltage-Gated CaBiochemistry · 2026Article
- Electrophysiological Mechanisms and Therapeutic Potential of Calcium Channels in Atrial Fibrillation.Reviews in cardiovascular medicine · 2025Review
- Structure-Function Diversity of Calcium-Binding Proteins (CaBPs): Key Roles in Cell Signalling and Disease.Cells · 2025Review
- Caldendrin Is a Repressor of PIEZO2 Channels and Touch Sensation in Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Tumor Suppressor Role of INPP4B in Chemoresistant Retinoblastoma.Journal of oncology · 2023Article
- Chemical shift assignments of the C-terminal domain of CaBP1 bound to the IQ-motif of voltage-gated CaBiomolecular NMR assignments · 2022Article
- NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors.Biochemistry · 2021Article
- Characterization of NCS1-InsP3R1 interaction and its functional significance.The Journal of biological chemistry · 2019Article
- Identification of key candidate genes and pathways in glioblastoma by integrated bioinformatical analysis.Experimental and therapeutic medicine · 2019Article
- Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019Review
- Structure and Function of IPCold Spring Harbor perspectives in biology · 2019Review
- Caldendrin and Calneurons-EF-Hand CaM-Like Calcium Sensors With Unique Features and Specialized Neuronal Functions.Frontiers in molecular neuroscience · 2019Review
- Dimerization of Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2018Review
- Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State.The Journal of biological chemistry · 2016Article
- Decalmodulation of Cav1 channels by CaBPs.Channels (Austin, Tex.) · 2016Review
- Sense and specificity in neuronal calcium signalling.Biochimica et biophysica acta · 2015Review
- Regulatory Mechanisms of Endoplasmic Reticulum Resident IP3 Receptors.Journal of molecular neuroscience : MN · 2015Review
- Structural insights into activation of the retinal L-type Ca²⁺ channel (Cav1.4) by Ca²⁺-binding protein 4 (CaBP4).The Journal of biological chemistry · 2014Article
- Chemistry and biology of the initial steps in vision: the Friedenwald lecture.Investigative ophthalmology & visual science · 2014Article
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7 authors.
Funding
Abstract
Calcium-binding protein 1 (CaBP1), a neuron-specific member of the calmodulin (CaM) superfamily, modulates Ca2+-dependent activity of inositol 1,4,5-trisphosphate receptors (InsP3Rs). Here we present NMR structures of CaBP1 in both Mg2+-bound and Ca2+-bound states and their structural interaction with InsP3Rs. CaBP1 contains four EF-hands in two separate domains. The N-domain consists of EF1 and EF2 in a closed conformation with Mg2+ bound at EF1. The C-domain binds Ca2+ at EF3 and EF4, and exhibits a Ca2+-induced closed to open transition like that of CaM. The Ca2+-bound C-domain contains exposed hydrophobic residues (Leu132, His134, Ile141, Ile144, and Val148) that may account for selective binding to InsP3Rs. Isothermal titration calorimetry analysis reveals a Ca2+-induced binding of the CaBP1 C-domain to the N-terminal region of InsP3R (residues 1-587), whereas CaM and the CaBP1 N-domain did not show appreciable binding. CaBP1 binding to InsP3Rs requires both the suppressor and ligand-binding core domains, but has no effect on InsP3 binding to the receptor. We propose that CaBP1 may regulate Ca2+-dependent activity of InsP3Rs by promoting structural contacts between the suppressor and core domains.
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