Molecular mechanisms underlying inhibition of protein phosphatases by marine toxins

Dawson, J.F.

doi:10.2741/a461

Cited by 54 publications

(28 citation statements)

References 34 publications

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“…on May 11, 2018 by guest http://mcb.asm.org/ both phosphatase activities at higher concentrations (11). Although the actual concentration of okadaic acid within the salivary glands cannot be controlled or assayed directly, we do observe an effect on the distribution of histone H3 dephosphorylation when salivary glands are incubated in culture medium containing 50 nM okadaic acid.…”

Section: Resultsmentioning

confidence: 66%

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Nowak

Pai

Corcés

2003

Molecular and Cellular Biology

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Transcriptional activation of the heat shock genes during the heat shock response in Drosophila has been intimately linked to phosphorylation of histone H3 at serine 10, whereas repression of non-heat-shock genes correlates with dephosphorylation of histone H3. It is then possible that specific kinase and/or phosphatase activities may regulate histone phosphorylation and therefore transcription activation and repression, respectively. We find that treatment of cells with strong phosphatase inhibitors interferes with the genome-wide dephosphorylation of histone H3 normally observed at non-heat-shock genes during heat shock. Mutants in protein phosphatase type 2A (PP2A) also display reduced genome-wide H3 dephosphorylation, and sites of H3 phosphorylation that do not contain heat shock genes remain transcriptionally active during heat shock in PP2A mutants. Finally, the SET protein, a potent and highly selective inhibitor of PP2A activity that inhibits PP2A-mediated dephosphorylation of Ser10-phosphorylated H3, is detected at transcriptionally active regions of polytene chromosomes. These results suggest that activation and repression of gene expression during heat shock might be regulated by changes in PP2A activity controlled by the SET protein.

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Section: Resultsmentioning

confidence: 66%

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Nowak

Pai

Corcés

2003

Molecular and Cellular Biology

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“…One of the dinoflagellate sources of OA, Prorocentrum lima, possesses both OA-sensitive PP-1c and PP-2Ac activities (Dawson and Holmes, 1999). The question arises of how this dinoflagellate avoids autotoxicity from OA.…”

Section: Okadaic Acidmentioning

confidence: 99%

Chemical Defenses: From Compounds to Communities

Paul

Arthur

Ritson‐Williams

et al. 2007

The Biological Bulletin

176

152

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“…The catalytic subunits of PP2A and PP1 are the only known targets of a set of toxins produced by a variety of organisms (7). The cell-permeable toxins, particularly okadaic acid, have been used extensively to study the biology of PP1 and PP2A.…”

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confidence: 99%

The 3D Structure of Protein Phosphatase 2A: New Insights into a Ubiquitous Regulator of Cell Signaling

Mumby

2007

ACS Chem. Biol.

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Molecular mechanisms underlying inhibition of protein phosphatases by marine toxins

Cited by 54 publications

References 34 publications

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Chemical Defenses: From Compounds to Communities

The 3D Structure of Protein Phosphatase 2A: New Insights into a Ubiquitous Regulator of Cell Signaling

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