phosphothreonine and cholesteryl-sulfate

phosphothreonine has been researched along with cholesteryl-sulfate* in 1 studies

Other Studies

1 other study(ies) available for phosphothreonine and cholesteryl-sulfate

Article	Year
Biochemical characterization of cholesterol-3-sulfate as the sole effector for the phosphorylation of HMG1 by casein kinase I in vitro. Biochemical and biophysical research communications, 2001, Volume: 281, Issue:5 Phosphorylation of high mobility group protein 1 (HMG1) by casein kinase I (CK-I) and potent effectors (inhibitors and activators) of this phosphorylation were investigated in vitro. We found that (i) CK-I phosphorylates specifically threonine residues on HMG1 when incubated with cholesterol-3-sulfate (CH-3S), but no phosphorylation of HMG1 is detected in the presence of other cholesterol related compounds or their sulfated derivatives; (ii) this phosphorylation is selectively inhibited by heparin, but stimulated significantly by 3',4',7-trihydroxy-isofavone at low doses (0.1-3 microM); and (iii) CH-3S directly induces a drastic conformational change in HMG1. The latter finding provides a mechanism to explain how CH-3S alone can induce the phosphorylation of HMG1 by CK-I in vitro. Topics: Animals; Casein Kinases; Cattle; Cholesterol Esters; Enzyme Activation; Flavonoids; Heparin; High Mobility Group Proteins; Phenols; Phosphorylation; Phosphothreonine; Polymers; Polyphenols; Protein Conformation; Protein Kinase Inhibitors; Protein Kinases	2001

Article

Year

Biochemical characterization of cholesterol-3-sulfate as the sole effector for the phosphorylation of HMG1 by casein kinase I in vitro.

Biochemical and biophysical research communications, 2001, Volume: 281, Issue:5

Phosphorylation of high mobility group protein 1 (HMG1) by casein kinase I (CK-I) and potent effectors (inhibitors and activators) of this phosphorylation were investigated in vitro. We found that (i) CK-I phosphorylates specifically threonine residues on HMG1 when incubated with cholesterol-3-sulfate (CH-3S), but no phosphorylation of HMG1 is detected in the presence of other cholesterol related compounds or their sulfated derivatives; (ii) this phosphorylation is selectively inhibited by heparin, but stimulated significantly by 3',4',7-trihydroxy-isofavone at low doses (0.1-3 microM); and (iii) CH-3S directly induces a drastic conformational change in HMG1. The latter finding provides a mechanism to explain how CH-3S alone can induce the phosphorylation of HMG1 by CK-I in vitro.

Topics: Animals; Casein Kinases; Cattle; Cholesterol Esters; Enzyme Activation; Flavonoids; Heparin; High Mobility Group Proteins; Phenols; Phosphorylation; Phosphothreonine; Polymers; Polyphenols; Protein Conformation; Protein Kinase Inhibitors; Protein Kinases

2001