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JCS ePress online publication date 13 Jul 2004
doi: 10.1242/jcs.01210

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Research Article

cAMP-induced degradation of cyclin D3 through association with GSK-3{beta}


Soheil Naderi, Kristine B. Gutzkow, Hege U. Låhne, Siri Lefdal, W. Johnathan Ryves, Adrian J. Harwood, and Heidi K. Blomhoff*
* Author for correspondence (e-mail: h.k.blomhoff{at}basalmed.uio.no)

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-3{beta} (GSK-3{beta})-mediated phosphorylation of cyclin D3 at Thr-283. Elevation of cAMP did not change the subcellular distribution of either cyclin D3 or GSK-3{beta}. However, cAMP promoted the interaction between cyclin D3 and GSK-3{beta} both in vitro and in vivo, indicating that GSK-3{beta}-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-3{beta} might phosphorylate unprimed substrates in vivo.


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