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Science 22 May 1998:
Vol. 280. no. 5367, pp. 1258 - 1261
DOI: 10.1126/science.280.5367.1258
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Reports

A Signaling Complex of Ca2+-Calmodulin-Dependent Protein Kinase IV and Protein Phosphatase 2A

Ryan S. Westphal, *dagger Kristin A. Anderson, * Anthony R. Means, Brian E. Wadzinski ddagger

Stimulation of T lymphocytes results in a rapid increase in intracellular calcium concentration ([Ca2+]i) that parallels the activation of Ca2+-calmodulin-dependent protein kinase IV (CaMKIV), a nuclear enzyme that can phosphorylate and activate the cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB). However, inactivation of CaMKIV occurs despite the sustained increase in [Ca2+]i that is required for T cell activation. A stable and stoichiometric complex of CaMKIV with protein serine-threonine phosphatase 2A (PP2A) was identified in which PP2A dephosphorylates CaMKIV and functions as a negative regulator of CaMKIV signaling. In Jurkat T cells, inhibition of PP2A activity by small t antigen enhanced activation of CREB-mediated transcription by CaMKIV. These findings reveal an intracellular signaling mechanism whereby a protein serine-threonine kinase (CaMKIV) is regulated by a tightly associated protein serine-threonine phosphatase (PP2A).

R. S. Westphal and B. E. Wadzinski, Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
K. A. Anderson and A. R. Means, Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
*   These authors contributed equally to this report.

dagger    Present address: Howard Hughes Medical Institute, Vollum Institute, Oregon Health Sciences University L-474, 3181 SW Sam Jackson Park Road, Portland, OR 97201, USA.

ddagger    To whom correspondence should be addressed.

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