RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca 2+ release

Randen L. Patterson, Damian B. Van Rossum, Roxanne K. Barrow, Solomon H. Snyder

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


RACK1 is not a G protein but closely resembles the heterotrimeric Gβ-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.

Original languageEnglish (US)
Pages (from-to)2328-2332
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number8
StatePublished - Feb 22 2004

All Science Journal Classification (ASJC) codes

  • General


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