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Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics

Corinna Bialojan, +1 more
- 15 Nov 1988 - 
- Vol. 256, Iss: 1, pp 283-290
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TLDR
Kinetic studies showed that okadaic acid acts as a non-competitive or mixed inhibitor on the okadaIC acid-sensitive enzymes.
Abstract
The inhibitory effect of a marine-sponge toxin, okadaic acid, was examined on type 1, type 2A, type 2B and type 2C protein phosphatases as well as on a polycation-modulated (PCM) phosphatase. Of the protein phosphatases examined, the catalytic subunit of type 2A phosphatase from rabbit skeletal muscle was most potently inhibited. For the phosphorylated myosin light-chain (PMLC) phosphatase activity of the enzyme, the concentration of okadaic acid required to obtain 50% inhibition (ID50) was about 1 nM. The PMLC phosphatase activities of type 1 and PCM phosphatase were also strongly inhibited (ID50 0.1-0.5 microM). The PMCL phosphatase activity of type 2B phosphatase (calcineurin) was inhibited to a lesser extent (ID50 4-5 microM). Similar results were obtained for the phosphorylase a phosphatase activity of type 1 and PCM phosphatases and for the p-nitrophenyl phosphate phosphatase activity of calcineurin. The following phosphatases were not affected by up to 10 microM-okadaic acid: type 2C phosphatase, phosphotyrosyl phosphatase, inositol 1,4,5-trisphosphate phosphatase, acid phosphatases and alkaline phosphatases. Thus okadaic acid had a relatively high specificity for type 2A, type 1 and PCM phosphatases. Kinetic studies showed that okadaic acid acts as a non-competitive or mixed inhibitor on the okadaic acid-sensitive enzymes.

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Type-2A protein phosphatase activity is required to maintain death receptor responsiveness.

TL;DR: It is demonstrated that the apoptosis mediated by Fas, TNF-α, and TRAIL in U937 cells is suppressed by calyculin A, an inhibitor of type-1 and type-2A protein phosphatases.
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Phosphatase 2A associated with polyomavirus small-T or middle-T antigen is an okadaic acid-sensitive tyrosyl phosphatase

TL;DR: The results indicate how middle-T/small-T might effect the activity of PP2A in polyoma virus-transformed cells and suggest that the same enzyme may possess dual specificity.
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Okadaic Acid Stimulates Glucose Transport in Rat Adipocytes by Increasing the Externalization Rate Constant of GLUT4 Recycling

TL;DR: It is suggested that insulin stimulates GLUT4 externalization by increasing the phosphorylation state of a serine/threonine phosphoprotein, probably by inhibiting protein phosphatase 1 or 2A.
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Calcium influx and protein phosphorylation mediate the metabolic stabilization of synaptic acetylcholine receptors in muscle

TL;DR: The pathway linking muscle activity and metabolic stabilization of synaptic AChRs in organ cultured rat muscle is investigated and findings are consistent with the notion that muscle activity initiates AChR stabilization via the activation of calcium-dependent protein phosphorylation reactions.
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Adrenocorticotropic hormone regulates the activities of the orphan nuclear receptor Nur77 through modulation of phosphorylation.

TL;DR: It is shown that ACTH regulates the activity of Nur77 at the level of phosphorylation, and it is proposed thatACTH treatment of Y1 cells results in modulation of the activities of both kinases and phosphatases, which, in turn, regulate the Activities of such transcription factors as Nur77.
References
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TL;DR: Examination of the amino acid sequences around each phosphorylation site does not support the idea that protein phosphatase specificity is determined by the primary structure in the immediate vicinity of the phosphorylated site, and demonstrates that proteinosphatase-1 and protein phosph atase 2A have very broad substrate specificities.
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