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RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca2+ release
Randen L. Patterson *,
Damian B. van Rossum *,
Roxanne K. Barrow *, and
Solomon H. Snyder * ¶
Departments of *Neuroscience, Pharmacology and Molecular Science, and Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205
Contributed by Solomon H. Snyder, December 30, 2003
RACK1 is not a G protein but closely resembles the heterotrimericG-subunit. RACK1 serves as a scaffold, linking protein kinaseC to its substrates. We demonstrate that RACK1 physiologicallybinds inositol 1,4,5-trisphosphate receptors and regulates Ca2+release by enhancing inositol 1,4,5-trisphosphate receptor bindingaffinity for inositol 1,4,5-trisphosphate. Overexpression ofRACK1 or depletion of RACK1 by interference RNA markedly augmentsor diminishes Ca2+ release, respectively, without affectingCa2+ entry. These findings establish RACK1 as a physiologicmediator of agonist-induced Ca2+ release.
DANGER, a Novel Regulatory Protein of Inositol 1,4,5-Trisphosphate-Receptor Activity.
D. B. van Rossum, R. L. Patterson, K.-H. Cheung, R. K. Barrow, V. Syrovatkina, G. S. Gessell, S. G. Burkholder, D. N. Watkins, J. K. Foskett, and S. H. Snyder (2006)
J. Biol. Chem.
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The Inositol 1,4,5-Trisphosphate Receptor (IP3R) and Its Regulators: Sometimes Good and Sometimes Bad Teamwork.