M phase-promoting factor: its identification as the M phase-specific H1 histone kinase and its activation by dephosphorylation. 1989

M Dorée, and J C Labbé, and A Picard
CNRS, Montpellier, France.

A major protein kinase independent of Ca2+, cyclic nucleotide or diacylglycerol, the activity of which becomes maximal when cells enter M phase, decreases at ana-telophase, and is low during interphase, has been purified to near homogeneity from starfish oocytes and its catalytic subunit identified as p34cdc2. M phase-promoting factor (MPF) was found to co-purify with the M phase-specific kinase throughout its purification. p34cdc2 does not have to be associated with any specific protein for expression of H1 histone kinase or MPF activities. When p34cdc2 is phosphorylated its protein kinase activity is inhibited, preventing entry into M phase, but once p34cdc2 becomes dephosphorylated, its protein kinase activity increases and M phase is initiated. A second peak of MPF activity was separated from p34cdc2 in the ammonium sulfate fraction treated with ATP-gamma-S. It induced p34cdc2 dephosphorylation and the concomitant stimulation of its kinase activity when injected in Xenopus or starfish oocytes.

UI MeSH Term Description Entries
D008938 Mitosis A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species. M Phase, Mitotic,Mitotic M Phase,M Phases, Mitotic,Mitoses,Mitotic M Phases,Phase, Mitotic M,Phases, Mitotic M
D009865 Oocytes Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM). Ovocytes,Oocyte,Ovocyte
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005260 Female Females
D006656 Protamine Kinase An aspect of protein kinase (EC 2.7.1.37) in which serine residues in protamines and histones are phosphorylated in the presence of ATP. Histone Kinase,Kinase, Histone,Kinase, Protamine
D000255 Adenosine Triphosphate An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013215 Starfish Echinoderms having bodies of usually five radially disposed arms coalescing at the center. Sea Star,Seastar,Starfishes,Sea Stars,Seastars

Related Publications

M Dorée, and J C Labbé, and A Picard
October 1998, Comparative biochemistry and physiology. Part C, Pharmacology, toxicology & endocrinology,
M Dorée, and J C Labbé, and A Picard
January 1989, Princess Takamatsu symposia,
M Dorée, and J C Labbé, and A Picard
March 1992, Journal of cell science,
M Dorée, and J C Labbé, and A Picard
April 1992, European journal of biochemistry,
M Dorée, and J C Labbé, and A Picard
August 1989, The EMBO journal,
M Dorée, and J C Labbé, and A Picard
September 2001, The Journal of biological chemistry,
M Dorée, and J C Labbé, and A Picard
February 1984, FEBS letters,
M Dorée, and J C Labbé, and A Picard
December 1990, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!