Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization

Article Abstract:

Glycogen synthase kinase-3beta (GSK-3beta) phosphorylates cyclin D1 on the carboxyl terminus (Thr-286) specifically and by doing so triggers rapid cyclin D1 turnover. Activity of GSK-3beta can be held back by signaling along a pathway that sequentially involves phosphatidylinositol-3-OH kinase (PI3K), Ras, and protein kinase B (Akt). The turnover of cyclin D1 is Ras dependent as its assembly is and mitogen regulated as a result. Proteolytic turnover and phosphorylation of cyclin D1 and its subcellular localization in cell division are connected by activity of GSK-3beta.

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Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors

Article Abstract:

Results reveal that INK4 inhibitor binding to the cyclin-dependent kinases 4 and 6 weakens the affinity of D-type cyclins to the enzyme as shown by the enzyme-cyclin-inhibitor complex crystal structure analysis. Data point out that the inhibition results from distortion of the ATP binding site and misalignment of catalytic residues.

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Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation

Article Abstract:

Results show that cyclin D1 transport from nucleus to cytoplasm during S phase of cell cycle is mediated by CRM1 nuclear exporting protein. Data further indicate that nuclear export activation of cyclin D1 occurs via threonine-286 phosphorylation, which in turn favors D1-CRMI complex formation.

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