ArticleThe Journal of biological chemistry2011
Structure of a Ca2+-myristoyl switch protein that controls activation of a phosphatidylinositol 4-kinase in fission yeast.
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 37 papers.
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Who cites it
37 citing papers in PubMed, 53 citations in OpenAlex.
- Myristoylated Neuronal Calcium Sensor-1 captures the preciliary vesicle at distal appendages.eLife · 2025Article
- Characterization of Pik1 function in fission yeast reveals its conserved role in lipid synthesis and not cytokinesis.Journal of cell science · 2023Article
- Myristoylated Neuronal Calcium Sensor-1 captures the ciliary vesicle at distal appendages.bioRxiv : the preprint server for biology · 2023Article
- Multilimbed membrane guanylate cyclase signaling system, evolutionary ladder.Frontiers in molecular neuroscience · 2022Review
- The function of apolipoproteins L (APOLs): relevance for kidney disease, neurotransmission disorders, cancer and viral infection.The FEBS journal · 2021Review
- Effects of Membrane and Biological Target on the Structural and Allosteric Properties of Recoverin: A Computational Approach.International journal of molecular sciences · 2019Article
- Crystal structure of a CaScientific reports · 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
- 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
- Temperature-Dependent Conformational Properties of Human Neuronal Calcium Sensor-1 Protein Revealed by All-Atom Simulations.The journal of physical chemistry. B · 2016Article
- Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State.The Journal of biological chemistry · 2016Article
- Structure and Calcium Binding Properties of a Neuronal Calcium-Myristoyl Switch Protein, Visinin-Like Protein 3.PloS one · 2016Article
- Integrative Signaling Networks of Membrane Guanylate Cyclases: Biochemistry and Physiology.Frontiers in molecular neuroscience · 2016Review
- Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics.PloS one · 2016Article
- Effects of the C-Terminal Tail on the Conformational Dynamics of Human Neuronal Calcium Sensor-1 Protein.The journal of physical chemistry. B · 2015Article
- Sense and specificity in neuronal calcium signalling.Biochimica et biophysica acta · 2015Review
- Protein and Signaling Networks in Vertebrate Photoreceptor Cells.Frontiers in molecular neuroscience · 2015Review
- ¹H, ¹³C, and ¹⁵N chemical shift assignments of neuronal calcium sensor protein, hippocalcin.Biomolecular NMR assignments · 2014Article
- Structural diversity of neuronal calcium sensor proteins and insights for activation of retinal guanylyl cyclase by GCAP1.Frontiers in molecular neuroscience · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Neuronal calcium sensor (NCS) proteins transduce Ca2+ signals and are highly conserved from yeast to humans. We determined NMR structures of the NCS-1 homolog from fission yeast (Ncs1), which activates a phosphatidylinositol 4-kinase. Ncs1 contains an α-NH2-linked myristoyl group on a long N-terminal arm and four EF-hand motifs, three of which bind Ca2+, assembled into a compact structure. In Ca2+-free Ncs1, the N-terminal arm positions the fatty acyl chain inside a cavity near the C terminus. The C14 end of the myristate is surrounded by residues in the protein core, whereas its amide-linked (C1) end is flanked by residues at the protein surface. In Ca2+-bound Ncs1, the myristoyl group is extruded (Ca2+-myristoyl switch), exposing a prominent patch of hydrophobic residues that specifically contact phosphatidylinositol 4-kinase. The location of the buried myristate and structure of Ca2+-free Ncs1 are quite different from those in other NCS proteins. Thus, a unique remodeling of each NCS protein by its myristoyl group, and Ca2+-dependent unmasking of different residues, may explain how each family member recognizes distinct target proteins.
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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.