Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-beta in cells lacking the CDK indicator p15

Article Abstract:

Recent research into the regulation of the activity of the cyclin-dependent kinases (CDKs) which control cell growth and division has found that the cytokine TGF-beta can lead to the inhibition of Cdk4 and Cdk6 by boosting their level of tyrosine phosphorylation. The ability of TGF-beta to prevent expression of the CDK tyrosine phosphatase Cdc25A leads to tyrosine phosphorylation and inactivation of Cdk4/6 in a human mammary epithelial cell line. Defects in TGF-beta antiproliferative responsiveness may result from a rise in Cdc25A activity, a factor which has been identified in breast cancer.

Enzyme inhibitors

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Crossing receptor boundaries

Article Abstract:

A receptor tyrosine kinase (Ret) is required for signaling by the glial-cell-line-derived neurotrophic factor (GDNF). The receptor-ligand binding involves the cell-surface membrane protein GDNF-alpha. Studies show that Ret expression induces GDNF binding. The binding of GDNF to Ret requires association of GDNF and GDNF-alpha, and Ret phosphorylation on tyrosine. The phenotypes of GDNF-deficient and Ret-deficient mice are similar. GDNF is a member of the transforming growth factor-beta family but its receptor is a tyrosine kinase rather than a serine/threonine kinase.

Ligand binding (Biochemistry), Cell receptors

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Partnership between DPC4 and SMAD proteins in TGF-beta signalling pathways

Article Abstract:

DPC4 is important for the function of Smad1 and Smad2 in distinct transforming growth factor pathways, signaling mesoderm formation in Xenopus embryos. SMAD is a set of evolutionary conserved proteins. It is also essential for pathways signaling antimitogenic and transcriptional responses in mammalian breast epithelial cells. The SMAD signalling network may be disabled in cancer cells that have lost DPC4 functioning.

Physiological aspects, Observations, Mesoderm

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