Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-52415
Dev Growth Differ 1988 Apr 01;302:197-207. doi: 10.1111/j.1440-169X.1988.00197.x.
Show Gene links Show Anatomy links

Does the M-Phase Promoting Factor (MPF) Activate a Major Ca2+ -and Cyclic Nucleotide-Independent Protein Kinase in Starfish Ocytes?: (cell cycle/protein kinase/starfish oocyte).

Labbe JC , Picard A , Doree M .


Abstract
In starfish, the activity of a major Ca2+ -and cyclic nuleotide-independent protein kinase has been shown to fluctuate in phase with that of MPF along meiotic and mitotic cell cycle (23, 25). Microinjection of α-naphthylphosphate (α-NP), a potent phosphatase inhibitor, increased considerably (from 15 to 546 picomoles/min/mg protein) the activity of this major cycling kinase in homogenates. Although this result supported the view that kinase phosphorylation might induce its own activation, this hypothesis was eliminated because injection of cytoplasm from hormone-stimulated enucleated oocytes, which contained the fully activated kinase but no MPF, failed to trigger kinase activation in recipient oocytes. In contrast, kinase activation was induced in recipient oocytes injected with either cytoplasm taken from nucleated maturing oocytes, which contained high MPF and kinase activities, or cytoplasm taken later from hormone-stimulated and ATP-γ-S-injected oocytes which contained high MPF but low kinase activites. These results indicate that inhibiting dephosphorylation of some regulatory protein activates the M-phase-specific protein kinase. The possibility that the M-phase or maturation-promoting factor (MPF) might be this regulatory protein is discussed.

PubMed ID: 37282239
Article link: Dev Growth Differ