Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

Article Abstract:

The amino acid sequence FXFP serves as docking site to mediate ERK nitrogen-activate protein (MAP) kinase binding to substrates in protein families. MAP kinases phosphorylate certain groups of substrate proteins. ERK substrates have been predicted and peptide inhibitors of ERK have been designed, based on findings including that that FXFP is specific for ERK, but that the D box mediates binding to ERK and JNK MAP kinase. It appears that partially overlapping substrate specificities of ERK and JNK come from recognition of unique shared docking sites.

United States, Observations, Evolution (Biology), Evolution, Protein kinases

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Cip/Kip proteins: more than just CDKs inhibitors

Article Abstract:

New studies have suggested that Cip/Kip proteins play additional roles outside of the nucleus (coqueret 2003). Emerging data suggests a role for cytoplasmic p27 Kip1 in the regulation of cell migration, independent of cyclin-CDK inhibition.

Cell migration

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Rhythmic control of AANAT translation by hnRNP Q in circadian melatonin production

Article Abstract:

The expression of AANAt protein is up regulated at night by rhythmic translation of AANAT mRNA by highly conserved IRES (internal ribosome entry site) element. This is essential for the circadian production of pineal melatonnin.

Circadian rhythms, Melatonin

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