Effects of Corticosterone on Phosphorylation of Rat Liver Nuclear Proteins in Vitro

Gd, Bottoms; Ra, Jungmann; Ev, Morse

doi:10.3181/00379727-144-37532

Cited by 7 publications

(1 citation statement)

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“…Nuclear phosphoproteins have been shown to possess the characteristics that one would expect of molecules whose function is involved in the modulation of gene expression. These characteristics include tissue and species specificity [34--36], changes throughout the cell cycle [7,10,37,38], the ability to bind to homologous DNA high rates of turnover, changes correlated with the metabolic state of the cell, and changes in both protein species and degree of phosphorylation induced by a variety of gene-activating stimuli such as hormones [3,6,11,39]. Differences in the phosphorylation of nuclear proteins have also been demonstrated during carcinogenesis [5,40] and viral transformation [41].…”

Section: Discussionmentioning

confidence: 99%

Partial fractionation and characterization of nuclear protein kinases in HeLa S3 cells

Thomson¹,

Mon²,

Stein³

et al. 1979

Cell Differentiation

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Section: Discussionmentioning

confidence: 99%

Partial fractionation and characterization of nuclear protein kinases in HeLa S3 cells

Thomson¹,

Mon²,

Stein³

et al. 1979

Cell Differentiation

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Phosphorylation of non-histone proteins in the regulation of chromosome structure and function

Kleinsmith

1975

J. Cell. Physiol.

144

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Non-histone chromosomal proteins are phosphorylated and dephosphorylated within the intact nucleus by two independent sets of reactions, a protein kinase reaction which transfers the terminal phosphate group of a variety of nucleoside and deoxynucleoside triphosphates to serine and threonine residues in the proteins, and a phosphatase reaction which cleaves these phosphoserine and phosphothreonine bonds and releases inorganic phosphate. Several lines of evidence are consistent with the hypothesis that the phosphorylation and dephosphorylation of these proteins is involved in gene control mechanisms, including the findings that phosphorylated non-histone proteins are highly heterogeneous and their phosphorylation patterns are tissue specific, changes in their phosphorylation correlate with changes in chromatin structure and gene acticity, addition of phosphorylated non-histone proteins increases RNA synthesis in vitro. and phosphorylated non-histone proteins bind specifically to DNA. Cyclic AMP has both stimulatory and inhibitory properties on non-histone protein phosphorylation, depending on the enzyme fraction and substrate employed A specific protein component whose phosphorylation is inhibited by cyclic AMP has been found to be associated with RNA polymerase. The cyclic AMP-induced decrease in the phosphorylation of this protein correlates with an enhancement of RNA synthesis in vitro. These results suggest that both phosphorylation and dephosphorylation of chromatin-associated proteins may be involved in the control of gene readout.

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Molecular Events in Lymphocyte Activation: Role of Nonhistone Chromosomal Proteins in Regulating Gene Expression

Decker

Marchalonis

1978

Contemporary Topics in Molecular Immunology

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Effects of Corticosterone on Phosphorylation of Rat Liver Nuclear Proteins in Vitro

Cited by 7 publications

References 0 publications

Partial fractionation and characterization of nuclear protein kinases in HeLa S3 cells

Partial fractionation and characterization of nuclear protein kinases in HeLa S3 cells

Phosphorylation of non-histone proteins in the regulation of chromosome structure and function

Molecular Events in Lymphocyte Activation: Role of Nonhistone Chromosomal Proteins in Regulating Gene Expression

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