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 journalArticle

77 Citations (Scopus)

Abstract

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
Volume101
Issue number8
DOIs
StatePublished - Feb 22 2004
Externally publishedYes

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Inositol 1,4,5-Trisphosphate Receptors
Inositol 1,4,5-Trisphosphate
RNA Interference
GTP-Binding Proteins
Protein Kinase C

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca 2+ release. / Patterson, Randen L.; Van Rossum, Damian B.; Barrow, Roxanne K.; Snyder, Solomon H.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, No. 8, 22.02.2004, p. 2328-2332.

Research output: Contribution to journalArticle

Patterson, Randen L. ; Van Rossum, Damian B. ; Barrow, Roxanne K. ; Snyder, Solomon H. / RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca 2+ release. In: Proceedings of the National Academy of Sciences of the United States of America. 2004 ; Vol. 101, No. 8. pp. 2328-2332.
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