FK506 binding protein associated with the calcium release channel (ryanodine receptor).

Jayaraman, Thottala; Brillantes, Anne Marie B; Timerman, Anthony P.; Fleischer, Sidney; Erdjument‐Bromage, Hediye; Tempst, Paul; Marks, Andrew R.

doi:10.1016/s0021-9258(19)50114-4

Cited by 481 publications

(61 citation statements)

References 32 publications

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“…137 Consistently, immunosuppressive drugs inhibiting FKBP12 (and also FKBP12.6) were able to cause arterial hypertension, reducing vasodilation and also acting on vasoconstriction. 138 3.2 FKBP12.6 FKBP12.6 shares 85% sequence homology with FKBP12 126,139 and also contains a single FK-506-binding domain. FKBP12.6 plays an important role in RyR2 stabilization 140,141 and colocalizes with RyR2 in the heart 142 and vascular tissues, where it is the predominant isoform.…”

Section: Fkbp12mentioning

confidence: 99%

Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases

Perrucci

Gowran

Zanobini

et al. 2015

Cardiovascular Research

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Peptidyl-prolyl cis-trans-isomerases are a highly conserved family of immunophilins. The three peptidyl-prolyl cis-trans-isomerase subfamilies are cyclophilins, FK-506-binding proteins, and parvulins. Peptidyl-prolyl cis-trans-isomerases are expressed in multiple human tissues and regulate different cellular functions, e.g. calcium handling, protein folding, and gene expression. Moreover, these subfamilies have been shown to be consistently involved in several cardiac and vascular diseases including heart failure, arrhythmias, vascular stenosis, endothelial dysfunction, atherosclerosis, and hypertension. This review provides a concise description of the peptidyl-prolyl cis-trans-isomerases and presents an incisive selection of studies focused on their relationship with cardiovascular diseases.

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Section: Fkbp12mentioning

confidence: 99%

Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases

Perrucci

Gowran

Zanobini

et al. 2015

Cardiovascular Research

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“…The degree of activation of RyRs during EC coupling depends on the strength of the signal from the DHPR, which is added to activity imposed by other regulatory factors such as ATP, Mg 2ϩ , FKBP12, and calmodulin (i.e., the background activity of the RyR). The resting background activity of the calcium release channel can be modulated by a variety of cytoplasmic factors including Ca 2ϩ and ATP (Meissner, 1994), by co-proteins such as FKBP12 (Jayaraman et al, 1992;Timerman et al, 1993;Ahern et al, 1994), by covalent modification with oxidation or nitrosylation (see review by Dulhunty et al, 2000;Hart, 2000;Eu et al, 2000), and by phosphorylation (Wang and Best, 1992;Hermann-Frank and Varsanyi, 1993;Hain et al, 1994;Sonnleitner et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Characteristics of Irreversible ATP Activation Suggest that Native Skeletal Ryanodine Receptors Can Be Phosphorylated via an Endogenous CaMKII

Dulhunty¹,

Laver

Curtis³

et al. 2001

Biophysical Journal

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Phosphorylation of skeletal muscle ryanodine receptor (RyR) calcium release channels by endogenous kinases incorporated into lipid bilayers with native sarcoplasmic reticulum vesicles was investigated during exposure to 2 mM cytoplasmic ATP. Activation of RyRs after 1-min exposure to ATP was reversible upon ATP washout. In contrast, activation after 5 to 8 min was largely irreversible: the small fall in activity with washout was significantly less than that after brief ATP exposure. The irreversible activation was reduced by acid phosphatase and was not seen after exposure to nonhydrolyzable ATP analogs. The data suggested that the channel complex was phosphorylated after addition of ATP and that phosphorylation reduced the RyR's sensitivity to ATP, adenosine, and Ca(2+). The endogenous kinase was likely to be a calcium calmodulin kinase II (CaMKII) because the CaMKII inhibitor KN-93 and an inhibitory peptide for CaMKII prevented the phosphorylation-induced irreversible activation. In contrast, phosphorylation effects remained unchanged with inhibitory peptides for protein kinase C and A. The presence of CaMKIIbeta in the SR vesicles was confirmed by immunoblotting. The results suggest that CaMKII is anchored to skeletal muscle RyRs and that phosphorylation by this kinase alters the enhancement of channel activity by ATP and Ca(2+).

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“…In comparison with calcineurin, the loss of function of FKBP12 and other members seems to have much fewer and less drastic impacts on both yeast and mammals. Aside from BMP receptors, FKBP12 has been reported to modulate calcium flux in inositol 1,4,5-trisphosphate and ryanodine receptors (Cameron et al, 1995;Jayaraman et al, 1992), suggesting that FK506 may affect vascular or cardiac smooth muscle contractility. However, calcineurin inhibition alone has been recognized as a key potentiator of hypertension (Hoorn et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

Activation of BMP Signaling by FKBP12 Ligands Synergizes with Inhibition of CXCR4 to Accelerate Wound Healing

Peiffer¹,

Ahmadi

et al. 2019

Cell Chemical Biology

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FK506 binding protein associated with the calcium release channel (ryanodine receptor).

Cited by 481 publications

References 32 publications

Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases

Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases

Characteristics of Irreversible ATP Activation Suggest that Native Skeletal Ryanodine Receptors Can Be Phosphorylated via an Endogenous CaMKII

Activation of BMP Signaling by FKBP12 Ligands Synergizes with Inhibition of CXCR4 to Accelerate Wound Healing

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