Mb. Meyers et al., CALCIUM-DEPENDENT TRANSLOCATION OF SORCIN TO MEMBRANES - FUNCTIONAL RELEVANCE IN CONTRACTILE TISSUE, FEBS letters, 357(3), 1995, pp. 230-234
Sorcin, a 22 kDa calcium binding protein present in abundance in cardi
ac tissue and in multi-drug resistant cells and previously described a
s a soluble protein, is now shown to undergo a calcium-dependent trans
location process from the cytosol to cellular membranes in both system
s. The translocation process takes place also in E. coli BL21 cells th
at express recombinant sorcin, r-sorcin, and can be exploited in the p
urification of the protein, Calcium binding to purified r-sorcin occur
s at micromolar concentrations of the metal and is accompanied by a co
nformational change that renders the protein soluble in the non-ionic
detergent Triton X-114. This finding suggests that lipids are the targ
et of sorcin on cellular membranes. The possible significance of the c
alcium-dependent translocation of sorcin in the specialized functions
of sorcin-expressing cells is discussed.