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RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca2+ release

PNAS, 24 February 2004
Vol. 101, Issue 8, p. 2328-2332
DOI: 10.1073/pnas.0308567100

RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca2+ release

  1. Randen L. Patterson * , ,
  2. Damian B. van Rossum * , ,
  3. Roxanne K. Barrow *, and
  4. Solomon H. Snyder * , , § ,
  1. Departments of *Neuroscience, Pharmacology and Molecular Science, and §Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205
  1. Contributed by Solomon H. Snyder, December 30, 2003

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.

Footnotes

  • To whom correspondence should be addressed at: Department of Neuroscience, Johns Hopkins University, 725 North Wolfe Street, 813 WBSB, Baltimore, MD 21205. E-mail: ssnyder{at}jhmi.edu.

  • R.L.P. and D.B.v.R. contributed equally to this work.

  • Abbreviations: IP3, inositol 1,4,5-trisphosphate; IP3R, IP3 receptor; Gβ, Gβ-subunit; siRNA, small interfering RNA; YFP, yellow fluorescent protein; aa, amino acids; HEK, human embryonic kidney.

Citation:

R. L. Patterson, D. B. van Rossum, R. K. Barrow, and S. H. Snyder, RACK1 binds to inositol 1,4,5-trisphosphate receptors and mediates Ca2+ release. PNAS 101, 2328-2332 (2004).

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