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Targeting of PKA, PKC and protein phosphatases to cellular microdomains

1999; Elsevier BV; Volume: 26; Issue: 5 Linguagem: Inglês

10.1054/ceca.1999.0072

1532-1991

Alistair T.R. Sim, John D. Scott,

Protein Tyrosine Phosphatases

The intracellular responses to many distinct extracellular signals involve the direction of broad-based protein kinases and protein phosphatases to catalyse quite specific protein phosphorylation/dephosphorylation events. It is now clear that such specificity is often achieved through subcellular targeting of distinct pools of kinase or phosphatase towards particular substrates at specific subcellular locations. Given the dynamic nature of protein phosphorylation reactions, coordinated control of both kinase and phosphatases is often required and complexes formed by common scaffold or targeting proteins exist to direct both kinase and phosphatase to the same subcellular location. In many cases more than one kinase or phosphatase is required and binding proteins which target more than one kinase or phosphatase have now been identified. This review summarizes recent findings relating to the concept of targeting PKA, PKC and the major serine/threonine phosphatases, PP1, PP2A and PP2B, through the formation of multi-enzyme signalling complexes.