Regulatory subunit of type II cAMP-dependent protein kinase as substrate and inhibitor of protein phosphatase-1 and -2A
- 3 March 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 197 (1-2) , 139-142
- https://doi.org/10.1016/0014-5793(86)80314-3
Abstract
The dissociated regulatory subunit (RII) of autophosphorylated cAMP-dependent protein kinase II was dephosphorylated by the catalytic subunits of protein phosphatase-1 and -2A (phosphatase-1c and -2Ac) and by a high-Mr, polycation-dependent form of phosphatase-2A (2A0) with Km values of 5,0.3 and 1 μM, respectively. Dissociation of protein kinase by cAMP preferentially increased the dephosphorylation of RII by phosphatase-1c, whereas polycations (histone H1 or polybrene) markedly stimulated phosphatase-2Ac and -2Ao even in the absence of cAMP. Thiophosphorylated RII inhibited the dephosphorylation of phosphorylase a by these phosphatases with half-maximum inhibitory concentrations of 0.1–0.36 μMKeywords
This publication has 13 references indexed in Scilit:
- Separation of rabbit liver latent and spontaneously active phosphorylase phosphatases by chromatography on heparin- SepharoseBiochemical and Biophysical Research Communications, 1985
- Heparin inhibits the activity of protein phosphatase‐1FEBS Letters, 1984
- The Protein Phosphatases Involved in Cellular Regulation. 6. Measurement of Type-1 and Type-2 Protein Phosphatases in Extracts of Mammalian Tissues; an Assessment of Their Physiological RolesEuropean Journal of Biochemistry, 1983
- A Kinetic Analysis of the Effects of Inhibitor-1 and Inhibitor-2 on the Activity of Protein Phosphatase-1European Journal of Biochemistry, 1983
- [18] Reversible autophosphorylation of type II cAMP-dependent protein kinase: Distinction between intramolecular and intermolecular reactionsPublished by Elsevier ,1983
- [7] Regulatory subunits of bovine heart and rabbit skeletal muscle cAMP-dependent protein kinase isozymesPublished by Elsevier ,1983
- Phosphorylation and dephosphorylation of the regulatory subunit of cyclic 3′,5′-monophosphate-dependent protein kinase (type II) in vivo and in vitroBiochimica et Biophysica Acta (BBA) - General Subjects, 1980
- Purification and Properties of Phosphorprotein Phosphatases with Different Substrate and Divalent Cation Specificities from Canine HeartEuropean Journal of Biochemistry, 1978
- Adenosine-3': 5'-Monophosphate-Binding Proteins from Bovine Kidney. Isolation by Affinity Chromatography and Limited Proteolysis of the Regulatory Subunit of Protein Kinase IIEuropean Journal of Biochemistry, 1978
- Single step purification of the catalytic subunit(s) of cyclic 3′,5′-adenosine monophosphate-dependent protein kinase(s) from rat muscleBiochemical and Biophysical Research Communications, 1976