ArticleThe Journal of biological chemistry2011
Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1).
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 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A meta-analysis of cerebrospinal fluid visinin-like protein-1 in alzheimers disease patients relative to healthy controls and mild cognitive impairment patients.Neurosciences (Riyadh, Saudi Arabia) · 2017Pooled it
- Visinin-like protein 1 disrupts calcium homeostasis and promotes atrial fibrillation in human and rodent models.Signal transduction and targeted therapy · 2026Article
- Defined culture conditions robustly maintain human stem cell pluripotency, highlighting a role for CaCommunications biology · 2025Article
- Visinin-like 1, a novel target gene of the Wnt/β-catenin signaling pathway, is involved in apoptosis resistance in colorectal cancer.Cancer medicine · 2023Article
- Heavy Metals and Essential Metals Are Associated with Cerebrospinal Fluid Biomarkers of Alzheimer's Disease.International journal of molecular sciences · 2022Article
- Zinc Modulation of Neuronal Calcium Sensor Proteins: Three Modes of Interaction with Different Structural Outcomes.Biomolecules · 2022Article
- Neural innervation as a potential trigger of morphological color change and sexual dimorphism in cichlid fish.Scientific reports · 2020Article
- A Novel Approach to Bacterial Expression and Purification of Myristoylated Forms of Neuronal Calcium Sensor Proteins.Biomolecules · 2020Article
- Functional Status of Neuronal Calcium Sensor-1 Is Modulated by Zinc Binding.Frontiers in molecular neuroscience · 2018Article
- Dimerization of Neuronal Calcium Sensor Proteins.Frontiers in molecular neuroscience · 2018Review
- Biophysical and functional characterization of hippocalcin mutants responsible for human dystonia.Human molecular genetics · 2017Article
- CIB1: a small protein with big ambitions.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Review
- Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.PloS one · 2016Article
- Oligomeric state regulated trafficking of human platelet-activating factor acetylhydrolase type-II.Biochimica et biophysica acta · 2015Article
- Protein and Signaling Networks in Vertebrate Photoreceptor Cells.Frontiers in molecular neuroscience · 2015Review
- Detection of genome-wide copy number variations in two chicken lines divergently selected for abdominal fat content.BMC genomics · 2014Article
- Article
- Translating neuronal activity at the synapse: presynaptic calcium sensors in short-term plasticity.Frontiers in cellular neuroscience · 2014Review
- Comparative phylogenomics of the CBL-CIPK calcium-decoding network in the moss Physcomitrella, Arabidopsis, and other green lineages.Frontiers in plant science · 2014Article
- Structural diversity of neuronal calcium sensor proteins and insights for activation of retinal guanylyl cyclase by GCAP1.Frontiers in molecular neuroscience · 2014Review
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4 authors.
Funding
Abstract
Visinin-like protein 1 (VILIP-1) belongs to the neuronal calcium sensor family of Ca(2+)-myristoyl switch proteins that regulate signal transduction in the brain and retina. Here we analyze Ca(2+) and Mg(2+) binding, characterize metal-induced conformational changes, and determine structural effects of myristoylation and dimerization. Mg(2+) binds functionally to VILIP-1 at EF3 (ΔH = +1.8 kcal/mol and K(D) = 20 μM). Unmyristoylated VILIP-1 binds two Ca(2+) sequentially at EF2 and EF3 (K(EF3) = 0.1 μM and K(EF2) = 1-4 μM), whereas myristoylated VILIP-1 binds two Ca(2+) with lower affinity (K(D) = 1.2 μM) and positive cooperativity (Hill slope = 1.5). NMR assignments and structural analysis indicate that Ca(2+)-free VILIP-1 contains a sequestered myristoyl group like that of recoverin. NMR resonances of the attached myristate exhibit Ca(2+)-dependent chemical shifts and NOE patterns consistent with Ca(2+)-induced extrusion of the myristate. VILIP-1 forms a dimer in solution independent of Ca(2+) and myristoylation. The dimerization site is composed of residues in EF4 and the loop region between EF3 and EF4, confirmed by mutagenesis. We present the structure of the VILIP-1 dimer and a Ca(2+)-myristoyl switch to provide structural insights into Ca(2+)-induced trafficking of nicotinic acetylcholine receptors.
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