Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases

Article Abstract:

The dephosphorylation of a Thr-169 phosphorylated form of Cdc28p in crude yeast lysates has been characterized in order to identify the Cdc28p phosphatase. Type 2C protein phosphatase(PP2C)-like activities take care of the dephosphorylation of Cdc29p in yeast extracts. Identification of the basic kinases and phosphatases acting on the major phosphorylation sites of the cyclin-dependent kinases (CDKs) controlling cell cycle progression has been completed with the determination of PP2Cs as the main protein phosphatases opposing Cdk-activating kinase (CAK).

Statistical Data Included, Cell cycle, Phosphatases

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The death domain kinase RIP has an essential role in DNA damage-induced NF-(kappa)B activation

Article Abstract:

The death domain RIP (receptor interacting protein) has been found to have a necessary function in DNA damage-induced NF-(kappa)B (a transcription factor) activation. W hen cells are exposed to genotoxic stress NF-(kappa)B is activated . DNA damage appears to trigger a cytoplasmic signal leading to IKK and NF-(kappa)B activation. RIP is the IKK upstream component.

Japan, DNA damage

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Translational control by TOR and TAP42 through dephosphorylation of eIF2(alpha) kinase GCN2

Article Abstract:

Translational control by TOR and TAP42, which takes place through dephosphorylation of eIF2(alpha) kinase GCN2, is discussed. It has been shown that rapamycin stimulates EIF2(alpha) phosphorylation by GCN2, with induction of GCN4 translation, while reducing Ser577 phosphorylation in nonstarved cells.

Rapamycin, Genetic translation, Translation (Genetics)

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