Calcium-dependent translocation of sorcin to membranes: functional relevance in contractile tissue.
Publication/Presentation Date
1-9-1995
Abstract
Sorcin, a 22 kDa calcium binding protein present in abundance in cardiac tissue and in multi-drug resistant cells and previously described as a soluble protein, is now shown to undergo a calcium-dependent translocation process from the cytosol to cellular membranes in both systems. The translocation process takes place also in E. coli BL21 cells that express recombinant sorcin, r-sorcin, and can be exploited in the purification of the protein. Calcium binding to purified r-sorcin occurs at micromolar concentrations of the metal and is accompanied by a conformational change that renders the protein soluble in the non-ionic detergent Triton X-114. This finding suggests that lipids are the target of sorcin on cellular membranes. The possible significance of the calcium-dependent translocation of sorcin in the specialized functions of sorcin-expressing cells is discussed.
Volume
357
Issue
3
First Page
230
Last Page
234
ISSN
0014-5793
Published In/Presented At
Meyers, M. B., Zamparelli, C., Verzili, D., Dicker, A. P., Blanck, T. J., & Chiancone, E. (1995). Calcium-dependent translocation of sorcin to membranes: functional relevance in contractile tissue. FEBS letters, 357(3), 230–234. https://doi.org/10.1016/0014-5793(94)01338-2
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
7835417
Department(s)
Administration and Leadership
Document Type
Article