Biochemistry (Easton), 2017-01, Vol.56 (2), p.411-420
2017
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Details
- Autor(en) / Beteiligte
- Titel
- Secretagogin Is a Redox-Responsive Ca 2+ Sensor
- Ist Teil von
- Biochemistry (Easton), 2017-01, Vol.56 (2), p.411-420
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2017
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Secretagogin (SCGN), a multifunctional, Ca binding, regulatory protein, known to regulate insulin release, has recently been implicated in the control of stress-related corticotropin-releasing hormone (CRH) secretion. Localization of SCGN to multiple intracellular (such as cytosol, nucleus, and endoplasmic reticulum) and extracellular sites appears to provide multifunctional capabilities; however, the structural elements conferring such a widespread cellular distribution to SCGN remain unidentified. We report that the spatial and functional attributes of SCGN plausibly originate from the interplay between Ca and its redox state. The mutation of selective Cys residues provides further insights into the origin and mode of redox responsiveness. In the reducing milieu, SCGN exhibits a higher affinity for Ca , and more stability than in the oxidizing environment, suggesting it is a redox-responsive Ca sensor protein, which is further supported by its response to dithiothreitol (reducing stress) in MIN6 cells. Our data provide a biophysical and biochemical explanation for the diverse localization of SCGN in the cellular scenario and beyond the cell.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0006-2960eISSN: 1520-4995DOI: 10.1021/acs.biochem.6b00761Titel-ID: cdi_crossref_primary_10_1021_acs_biochem_6b00761
- Format
- –
- Schlagworte
- Animals, Binding Sites, Calcium - chemistry, Calcium - metabolism, Cell Line, Tumor, Cell Nucleus - drug effects, Cell Nucleus - metabolism, Cloning, Molecular, Cysteine - chemistry, Cysteine - metabolism, Cytosol - drug effects, Cytosol - metabolism, Dithiothreitol - pharmacology, Endoplasmic Reticulum - drug effects, Endoplasmic Reticulum - metabolism, Escherichia coli - genetics, Escherichia coli - metabolism, Gene Expression Regulation, Insulin-Secreting Cells - drug effects, Insulin-Secreting Cells - metabolism, Mice, Models, Molecular, Oxidation-Reduction, Protein Binding, Protein Domains, Protein Multimerization, Protein Structure, Secondary, Recombinant Proteins - chemistry, Recombinant Proteins - genetics, Recombinant Proteins - metabolism, Secretagogins - chemistry, Secretagogins - genetics, Secretagogins - metabolism