Biochemical and Biophysical Research Communications
Sequence analysis of the ryanodine receptor: Possible association with a 12K, FK506-binding immunophilin/protein kinase C inhibitor
References (17)
Physiol. Rev
(1984)- et al.
J. Biol. Chem
(1990) - et al.
Nature
(1989) - et al.
- et al.
- et al.
Nature
(1990) Cell
(1991)- et al.
Eur. J. Biochem
(1990)
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Ryanodine receptors: Allosteric ion channel giants
2015, Journal of Molecular BiologyCitation Excerpt :FKBP12 and FKBP12.6 are small proteins (12 and 12.6 kDa, respectively) that are targeted by the immunosuppressive agents rapamycin and FK506 and owe their name to binding the latter (FK506-binding protein). They have a compact fold [156] and co-purify readily with RyRs in a 4:1 stoichiometry (one FKBP per RyR subunit) [157,158]. Surface plasmon resonance experiments have shown that FKBPs have a very high affinity for RyRs, with a Kd of ~ 1 nM for open channels, but they bind orders of magnitude stronger to closed channels [159].
FK506 binding proteins: Cellular regulators of intracellular Ca <sup>2+</sup> signalling
2013, European Journal of PharmacologyCitation Excerpt :Yet, their role in intracellular Ca2+ signalling is controversial; FKBPs reportedly increase, decrease or have no effect on ryanodine receptor- or IP3 receptor-mediated Ca2+ release in various cell types examined, including smooth muscle. A physiological interaction between the accessory protein, FKBP12, and the skeletal muscle ryanodine RyR1 receptor isoform is well established (Carmody et al., 2001; Collins, 1991; Jayaraman et al., 1992; Lehnart et al., 2003; Samso et al., 2006; Wen et al., 2012). The molecular interaction between FKBP12 and the ryanodine receptor stabilizes the closed state of the channel (Ahern et al., 1994, 1997; Brillantes et al., 1994; Marx et al., 1998; Marx et al., 2001; McCall et al., 1996; Ondrias et al., 1998; Timerman et al., 1993).
Ryanodine receptor-mediated arrhythmias and sudden cardiac death
2009, Pharmacology and TherapeuticsCitation Excerpt :These 12 kDa proteins are thought to be potent and important regulators of RyR function. They bind with high affinity in both the open or closed state of the channel although the affinity is greater when the channel is closed (Jones et al., 2005b) and indeed interaction with the FKBP12 protein was first identified by its persistent co-purification with RyR1 channels (Collins, 1991; Jayaraman et al., 1992). One FKBP12 interacts with one RyR1 subunit (Jayaraman et al., 1992; Timerman et al., 1995) and topological analysis has shown four FKBP12 molecules bound symmetrically proximal to the N-terminus (Wagenknecht et al., 1997).
Elucidation of the ryanodine-sensitive Ca<sup>2+</sup> release mechanism of rat pancreatic acinar cells: Modulation by cyclic ADP-ribose and FK506
2004, Biochimica et Biophysica Acta - Molecular Cell ResearchCalcineurin inhibitors and the generalization of the presenting protein strategy
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