ReviewBiochimica et biophysica acta2012
Molecular structure and target recognition of neuronal calcium sensor proteins.
Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 85 citations in OpenAlex.
- Article
- Zinc Modulation of Neuronal Calcium Sensor Proteins: Three Modes of Interaction with Different Structural Outcomes.Biomolecules · 2022Article
- Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.International journal of molecular sciences · 2021Article
- Functional Interaction between Transient Receptor Potential V4 Channel and Neuronal Calcium Sensor 1 and the Effects of Paclitaxel.Molecular pharmacology · 2021Article
- Complex precursor structures of cytolytic cupiennins identified in spider venom gland transcriptomes.Scientific reports · 2021Article
- Pharmacological Approaches for the Modulation of the Potassium Channel KInternational journal of molecular sciences · 2021Review
- Bringing the CaOpen biology · 2021Article
- Experimental Insight into the Structural and Functional Roles of the 'Black' and 'Gray' Clusters in Recoverin, a Calcium Binding Protein with Four EF-Hand Motifs.Molecules (Basel, Switzerland) · 2019Article
- Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019Review
- NaPi-IIa interacting partners and their (un)known functional roles.Pflugers Archiv : European journal of physiology · 2019Review
- Evolutionary-Conserved Allosteric Properties of Three Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2019Article
- Evolution of the calcium feedback steps of vertebrate phototransduction.Open biology · 2018Article
- Novel approaches to probe the binding of recoverin to membranes.European biophysics journal : EBJ · 2018Article
- Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization.Frontiers in molecular neuroscience · 2018Article
- Dimerization of Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2018Review
- Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality.ACS central science · 2017Article
- Response of turkey muscle satellite cells to thermal challenge. I. transcriptome effects in proliferating cells.BMC genomics · 2017Article
- Interference of the complex between NCS-1 and Ric8a with phenothiazines regulates synaptic function and is an approach for fragile X syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Human Neuronal Calcium Sensor-1 Protein Avoids Histidine Residues To Decrease pH Sensitivity.The journal of physical chemistry. B · 2017Article
- Purification of cone outer segment for proteomic analysis on its membrane proteins in carp retina.PloS one · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundNeuronal calcium sensor (NCS) proteins, a sub-branch of the calmodulin superfamily, are expressed in the brain and retina where they transduce calcium signals and are genetically linked to degenerative diseases. The amino acid sequences of NCS proteins are highly conserved but their physiological functions are quite distinct. Retinal recoverin and guanylate cyclase activating proteins (GCAPs) both serve as calcium sensors in retinal rod cells, neuronal frequenin (NCS1) modulate synaptic activity and neuronal secretion, K+ channel interacting proteins (KChIPs) regulate ion channels to control neuronal excitability, and DREAM (KChIP3) is a transcriptional repressor that regulates neuronal gene expression. SCOPE OF REVIEW: Here we review the molecular structures of myristoylated forms of NCS1, recoverin, and GCAP1 that all look very different, suggesting that the sequestered myristoyl group helps to refold these highly homologous proteins into very different structures. The molecular structure of NCS target complexes have been solved for recoverin bound to rhodopsin kinase, NCS-1 bound to phosphatidylinositol 4-kinase, and KChIP1 bound to A-type K+ channels. MAJOR
conclusionsWe propose the idea that N-terminal myristoylation is critical for shaping each NCS family member into a unique structure, which upon Ca2+-induced extrusion of the myristoyl group exposes a unique set of previously masked residues, thereby exposing a distinctive ensemble of hydrophobic residues to associate specifically with a particular physiological target. This article is part of a Special Issue entitled Biochemical, biophysical and genetic approaches to intracellular calcium signaling.
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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.