Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 101, Issue 8, Pages 2328-2332Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0308567100
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Funding
- NIDA NIH HHS [DA-00074, DA-000266, K05 DA000074, P50 DA000266] Funding Source: Medline
- NIH HHS [NH65090] Funding Source: Medline
- NIMH NIH HHS [R01 MH018501, R37 MH018501, MH-18501] Funding Source: Medline
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RACK1 is not a G protein but closely resembles the heterotrimeric Gbeta-subunit. RACK1 serves as a scaffold, linking protein kinase C to its substrates. We demonstrate that RACK1 physiologically binds inositol 1,4,5-trisphosphate receptors and regulates Ca2+ release by enhancing inositol 1,4,5-trisphosphate receptor binding affinity for inositol 1,4,5-trisphosphate. Overexpression of RACK1 or depletion of RACK1 by interference RNA markedly augments or diminishes Ca2+ release, respectively, without affecting Ca2+ entry. These findings establish RACK1 as a physiologic mediator of agonist-induced Ca2+ release.
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