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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
Author(s) -
PICARD ANDRÉ,
LABBÉ JEANCLAUDE,
PEAUCELLIER GÉRARD,
BOUFFANT FRANÇOISE,
PEUCH CHRISTIAN,
DOREE MARCEL
Publication year - 1987
Publication title -
development, growth and differentiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.864
H-Index - 66
eISSN - 1440-169X
pISSN - 0012-1592
DOI - 10.1111/j.1440-169x.1987.00093.x
Subject(s) - maturation promoting factor , protein kinase a , cyclin dependent kinase 2 , microbiology and biotechnology , cgmp dependent protein kinase , biology , ask1 , mitogen activated protein kinase kinase , cell cycle , protein phosphorylation , cyclin dependent kinase 3 , mitosis , kinase , chemistry , cyclin dependent kinase 1 , biochemistry , cell
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 Ca 2+ . 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.