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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein.

FK506-binding protein (FKBP12) was originally identified as the cytosolic receptor for the immunosuppressant drugs FK506 and rapamycin. The cellular function of FKBP12, a ubiquitously expressed 12,000-dalton proline isomerase, has been unknown. FKBP12 copurifies with the 565,000-dalton ryanodine receptor (RyR), four of which form intracellular Ca2+ release channels of the sarcoplasmic and endoplasmic reticula. By coexpressing the RyR and FKBP12 in insect cells, we have demonstrated that FKBP12 modulates channel gating by increasing channels with full conductance levels (by > 400%), decreasing open probability after caffeine activation (from 0.63 +/- 0.09 to 0.04 +/- 0.02), and increasing mean open time (from 4.4 +/- 0.6 ms to 75 +/- 41 ms). FK506 or rapamycin, inhibitors of FKBP12 isomerase activity, reverse these stabilizing effects. These results provide the first natural cellular function for FKBP12, and establish that the functional Ca2+ release channel complex includes FKBP12.[1]


  1. Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein. Brillantes, A.B., Ondrias, K., Scott, A., Kobrinsky, E., Ondriasová, E., Moschella, M.C., Jayaraman, T., Landers, M., Ehrlich, B.E., Marks, A.R. Cell (1994) [Pubmed]
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