Changes in the Activity of the Maturation-Promoting Factor Are Correlated with Those of a Major Cyclic AMP and Calcium-Independent Protein Kinase During the First Mitotic Cell Cycles in the Early Starfish Embryo. (cell cycle/maturation-promoting factor/protein kinase/protein synthesis/starfish)
Autor: | Christian Le Peuch, Françoise Le Bouffant, Gerard Peaucellier, Jean-Claude Labbé, André Picard, Marcel Dorée |
---|---|
Rok vydání: | 1987 |
Předmět: |
Cyclin-dependent kinase 1
urogenital system Akt/PKB signaling pathway Cyclin-dependent kinase 2 Cyclin-dependent kinase 3 Maturation promoting factor Cell Biology Biology Cell biology Biochemistry biology.protein Protein phosphorylation Protein kinase A cGMP-dependent protein kinase reproductive and urinary physiology Developmental Biology |
Zdroj: | Development, Growth and Differentiation. 29:93-103 |
ISSN: | 1440-169X 0012-1592 |
DOI: | 10.1111/j.1440-169x.1987.00093.x |
Popis: | Many studies suggest that MPF activation depends on protein phosphorylation or that MPF is itself a protein kinase. In the present report, cyclic variations of MPF activity have been correlated in vivo with changes in the extent of protein phosphorylation or in vitro with changes of a major protein kinase during the first cell cycles of fertilized starfish eggs. This cycling protein kinase neither requires cAMP nor Ca2+. Neither colchicine nor aphidicoline, which inhibits cleavage and chromosome replication respectively, was found to suppress the synchronous and cyclic variations of both MPF and protein kinase activities. Protein synthesis was found to be required for both MPF and protein kinase activities to reappear after their simultaneous drop at the time of mitotic or meiotic cleavages. Production of either MPF or protein kinase activities is not the immediate result of protein synthesis since there is a delay at each cell cycle between the time when protein synthesis is required and the time when both MPF and protein kinase activities are produced. This suggests that both MPF and protein kinase activities might involve some post-translational modification of a precursor protein synthesized during the preceeding cell cycle. |
Databáze: | OpenAIRE |
Externí odkaz: |