Work

Reconstitution of p21ras-dependent and -independent mitogen-activated protein kinase activation in a cell-free system.

Year: 1993

Type: article

Abstract: In Xenopus oocytes, mitogen-activated protein (MAP) kinase can be activated by progesterone treatment or by microinjection of cyclin A, both of which lead to activation of the cdc2 protein kinase. The tyrosine kinase pp60v-src has previously been shown to accelerate progesterone-induced oocyte maturation and to increase the phosphorylation of ribosomal protein S6 by pp90rsk, most likely by activating MAP kinase. In extracts of resting oocytes, MAP kinase kinase and MAP kinase were activated by addition of pp60v-src or cyclin A. Activation by pp60v-src was blocked by a dominant-negative p21ras protein (RAST), but activation by cyclin A/cdc2 was unaffected. Thus these two pathways that converge at MAP kinase kinase but are clearly divergent upstream of a p21ras-dependent step can be studied in a cell-free system.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(20)80676-0

Authors: B VanRenterghem, J.B. Gibbs, J.L. Maller

Institutions: Howard Hughes Medical Institute, University of Colorado Anschutz, University of Colorado Denver

Language: English

Topic: Protein Kinase Regulation and GTPase Signaling

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institutes of Health, National Institute of General Medical Sciences, National Institute of Diabetes and Digestive and Kidney Diseases