ArticlePloS one2016
Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- NCS-1 protein regulates TRPA1 channel through the PI3K pathway in breast cancer and neuronal cells.Journal of physiology and biochemistry · 2024Article
- Distinct mechanism of TbPhysical chemistry chemical physics : PCCP · 2023Article
- Nanomolar affinity of EF-hands in neuronal calcium sensor 1 for bivalent cations Pb2+, Mn2+, and Hg2.Metallomics : integrated biometal science · 2022Article
- CaProtein science : a publication of the Protein Society · 2022Article
- Exonic splicing code and protein binding sites for calcium.Nucleic acids research · 2022Article
- Mechanism of ZnBiomolecules · 2021Article
- A Novel Approach to Bacterial Expression and Purification of Myristoylated Forms of Neuronal Calcium Sensor Proteins.Biomolecules · 2020Article
- Neuronal Calcium Sensor 1 is up-regulated in response to stress to promote cell survival and motility in cancer cells.Molecular oncology · 2020Article
- Calcium Sensors in Neuronal Function and Dysfunction.Cold Spring Harbor perspectives in biology · 2019Review
- NCS-1 is a regulator of calcium signaling in health and disease.Biochimica et biophysica acta. Molecular cell research · 2018Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Neuronal calcium sensor-1 (NCS-1 Var1) is a calcium-binding protein expressed in most tissues. We examined a poorly characterized variant of NCS-1 (Var2), identified only in humans where the N-terminal 22 amino acid residues of native NCS-1(MGKSNSKLKPEVVEELTRKTY) were replaced with 4 different residues (MATI). Because alterations in the level of expression of NCS-1 Var1 and the expression of NCS-1 variants have been correlated with several neurological diseases, the relative expression and functional role of NCS-1 Var2 was examined. We found that NCS-1 Var2 mRNA levels are not found in mouse tissues and are expressed at levels ~1000-fold lower than NCS-1 Var1 in three different human cell lines (SHSY5Y, HEK293, MB231). Protein expression of both variants was only identified in cell lines overexpressing exogenous NCS-1 Var2. The calcium binding affinity is ~100 times weaker in purified NCS-1 Var2 than NCS-1 Var1. Because truncation of NCS-1 Var1 has been linked to functional changes in neurons, we determined whether the differing properties of the NCS-1 variants could potentially contribute to the altered cell function. In contrast to previous reports showing that overexpression of NCS-1 Var1 increases calcium-dependent processes, functional differences in cells overexpressing NCS-1 Var2 were undetectable in assays for cell growth, cell death and drug (paclitaxel) potency. Our results suggest that NCS-1 Var1 is the primary functional version of NCS-1.
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