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Casein Kinase II as a Potentially Important Enzyme Concerned with Signal Transduction

1988; Cold Spring Harbor Laboratory Press; Volume: 53; Linguagem: Inglês

10.1101/sqb.1988.053.01.012

1943-4456

E G Krebs, Robert N. Eisenman, E.A. Kijenzel, David W. Litchfield, Fred J. Lozeman, Bernhard Lüscher, J Sommercorn,

Phytase and its Applications

Several of the effects of insulin and other growth factors whose receptors are protein tyrosine kinases are made manifest as a result of changes in the state of protein serine (threonine) phosphorylation involving certain cellular proteins (Denton 1986). It is even possible that all of the effects of such agents might be mediated in this manner (Krebs 1985). Such a scheme would provide an attractive mechanism that could explain the pleotypic action of these growth factors inasmuch as the protein serine (threonine) phosphorylation-dephosphorylation network is complex, involving a vast array of kinases and phosphatases that impinge on potential protein substrates in all parts of the cell (Edelman et al. 1987). Protein tyrosine phosphorylation is much less extensive than protein serine (threonine) phosphorylation (Hunter and Cooper 1981), but, as a result of coupling between the two systems, signals that give rise to changes in tyrosine phosphorylation could be amplified and widely...