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Cited by 1,978

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

PKA Phosphorylation Dissociates FKBP12.6 from the Calcium Release Channel (Ryanodine Receptor)

Open access
Marx, Steven O, Reiken, Steven, Hisamatsu, Yuji, Jayaraman, Thotalla, Burkhoff, Daniel, Rosemblit, Nora, Marks, Andrew R·2000·Cell
DOI 10.1016/s0092-8674(00)80847-8
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Abstract

The ryanodine receptor (RyR)/calcium release channel on the sarcoplasmic reticulum (SR) is the major source of calcium (Ca2+) required for cardiac muscle excitation-contraction (EC) coupling. The channel is a tetramer comprised of four type 2 RyR polypeptides (RyR2) and four FK506 binding proteins (FKBP12.6). We show that protein kinase A (PKA) phosphorylation of RyR2 dissociates FKBP12.6 and regulates the channel open probability (Po). Using cosedimentation and coimmunoprecipitation we have defined a macromolecular complex comprised of RyR2, FKBP12.6, PKA, the protein phosphatases PP1 and PP2A, and an anchoring protein, mAKAP. In failing human hearts, RyR2 is PKA hyperphosphorylated, resulting in defective channel function due to increased sensitivity to Ca2+-induced activation.

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Crossref · 10.1016/s0092-8674(00)80847-8

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Metadata

Authors
Marx, S. O., Reiken, S., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R.
Venue
Cell
Publisher
Elsevier BV
Published
2000-05
Volume
101
Issue
4
Pages
365-376
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/s0092-8674(00)80847-8
OpenAlex
W2140313980
Cited by
1,978
References
1
FWCI
68.39
Type
journal article
Language
en
Open access
hybrid

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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