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XB-ART-28270
Mol Cell Biol 1987 Feb 01;72:760-8.
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Metaphase protein phosphorylation in Xenopus laevis eggs.

Lohka MJ , Kyes JL , Maller JL .


Abstract
Cytoplasmic extracts of metaphase (M-phase)-arrested Xenopus laevis eggs support nuclear envelope breakdown and chromosome condensation in vitro. Induction of nuclear breakdown is inhibited by AMPP(NH)P, a nonhydrolyzable ATP analog, but not by ATP or gamma-S-ATP, a hydrolyzable ATP analog, suggesting that protein phosphorylation may be required for M-phase nuclear events in vitro. By addition of [gamma-32P]ATP, we have identified in cytoplasmic extracts and in intact eggs at least six phosphoproteins that are present during M-phase but absent in G1/S-phase. These phosphoproteins also appear in response to partially purified preparations of maturation-promoting factor. A subset of these proteins are thiophosphorylated by gamma-S-ATP under conditions that promote nuclear envelope breakdown and chromosome condensation. Each of these proteins is phosphorylated on serine and threonine, and one, a 42-kilodalton protein, is also phosphorylated on tyrosine both in extracts and in intact eggs. These results indicate that activation of protein kinases accounts for at least part of the increased phosphorylation in M-phase and that both protein-serine-threonine kinases and protein-tyrosine kinases may play a role in controlling M-phase nuclear behavior.

PubMed ID: 3821728
PMC ID: PMC365132
Article link: Mol Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: cdk1

References [+] :
Burke, A cell free system to study reassembly of the nuclear envelope at the end of mitosis. 1986, Pubmed