What goes up must come down

Article Abstract:

Eukaryotic cells uses reversible protein phosphorylation to adjust their metabolism, growth and differentiation. Westphal and colleagues and Camps and colleagues have reported a molecular device for feedback control of kinase signalling pathways, where a protein kinase, regulated by protein phosphorylation, becomes the substrate of a certain protein phosphatase. Westphal and colleagues report the interaction between CA(super2+)-calmodulin-dependent protein kinase IV and the protein phosphatase 2A (PP2A). Camps and colleagues describe the interaction between MKP-3, the dual-specificity protein phosphatase and its substrate, ERK2.

Eukaryotic cells, Cells (Biology), Eukaryotes, Cellular signal transduction, Phosphatases

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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

Article Abstract:

An insulin-stimulated protein kinase B from L6 myotubes inactivates glycogen synthase kinase-3 (GSK3)-alpha and GSK3-beta in vitro. Agents responsible for blocking the stimulation of MAP kinase-activated protein kinase and p70(super S6k) by insulin are unable to inhibit the phosphorylation of GSK3. Activation of L6 myotubes with insulin in the presence of PD98059 and rapamycin enhances 32P-labeling of GSK3-alpha and GSK3-beta by 60%-100%. The phosphorylation site acts as the third residue corresponding to the GSK3-alpha and GSK3-beta.

Analysis, Physiological aspects, Phosphorylation, Insulin

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Pleckstrin domain homology

Article Abstract:

Pleckstrin, a protein kinase C substrate of platelets, consists of N- and C-terminal domains having similar amino acid chains. The discovery of the significance of proteins in cytoskeletal function indicates the similarity between pleckstrin homology (PH) domain and SH2 and SH3 domains. It is possible that the pleckstrin phosphorelation controls PH interaction with other proteins, and these proteins help in signal transmission resulting in the secretion of platelet granule constituents.

Composition, Letter to the Editor

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