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First published online 13 July 2004
doi: 10.1242/jcs.01210

Journal of Cell Science 117, 3769-3783 (2004)
Published by The Company of Biologists 2004
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Research Article

cAMP-induced degradation of cyclin D3 through association with GSK-3ß

Soheil Naderi1,*, Kristine B. Gutzkow1,*, Hege U. Låhne1, Siri Lefdal1, W. Johnathan Ryves2, Adrian J. Harwood2 and Heidi K. Blomhoff1,{ddagger}

1 Department of Medical Biochemistry, University of Oslo, P.O. Box 1112 Blindern, Oslo, N-0317, Norway
2 MRC Laboratory for Molecular Cell Biology and Department of Biology, University College London, Gower Street, London, WC1E 6BT, UK

{ddagger} Author for correspondence (e-mail: h.k.blomhoff{at}basalmed.uio.no)

Accepted 9 March 2004

In this study we report a new mechanism whereby cyclic AMP (cAMP) regulates the cell-cycle machinery. We demonstrate that elevation of intracellular levels of cAMP promotes degradation of cyclin D3 in proteasomes, and that this occurs via glycogen synthase kinase-3ß (GSK-3ß)-mediated phosphorylation of cyclin D3 at Thr-283. Elevation of cAMP did not change the subcellular distribution of either cyclin D3 or GSK-3ß. However, cAMP promoted the interaction between cyclin D3 and GSK-3ß both in vitro and in vivo, indicating that GSK-3ß-mediated phosphorylation of cyclin D3 might require the association between the two proteins. These results demonstrate how cAMP enhances degradation of cyclin D3. Furthermore, we provide evidence for a novel mechanism by which GSK-3ß might phosphorylate unprimed substrates in vivo.

Key words: cAMP, Cyclin D3, GSK-3ß, Degradation




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