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PubMed1988

Activation of myelin basic protein kinases during echinoderm oocyte maturation and egg fertilization.

At least five activated protein kinases were detectable in soluble extracts from maturing as compared to immature sea star oocytes. These kinases could be distinguished on the basis of the time courses of their activation following exposure of the oocytes to 1-methyladenine, their substrate specificities, and their chromatographic properties on DEAE-Sephacel and Sephacryl S-200. A histone H1 kinase (HH1K) (Mr 110,000) underwent maximal activation near the time of 1-methyladenine-induced germinal vesicle breakdown (GVBD). When myelin basic protein (MBP) was used as a substrate, HH1K and two additional kinases (MBPK-I and MBPK-II) were detectable. MBPK-II (Mr 110,000) was fully activated at the time of GVBD, whereas peak activation of MBPK-I (Mr 45,000) occurred after this event. Two "ribosomal protein S6 kinases" (S6K-I and S6K-II) could be detected with a synthetic peptide (RRLSSLRA), which was patterned after a major phosphorylation site in S6. The two S6 kinases (Mr 110,000 for both) underwent activation post-GVBD. HH1K and S6K-I coeluted from DEAE-Sephacel at a conductivity of 5.5-6.0 mmho, whereas MBPK-I, MBPK-II, and S6K-II coeluted from this resin in a second peak at a conductivity = 10-11 mmho. The HH1K and MBPK-II activities both declined prior to the emission of the first polar body (i.e., meiotic cell division), but the MBPK-I, S6K-I, and S6K-II activities remained elevated during this time. The activities of these kinases were also examined during the early cell divisions in sea urchin embryos. Within 5 min after fertilization, the high level of MBPK-I activity in sea urchin eggs rapidly declined. However, along with the HH1K and MBPK-II activities, the MBPK-I activity was transiently increased prior to each cell division. No appreciable postfertilization changes in the S6K-I and S6K-II activities were apparent during the first three cycles of cell division.

Animals↗
PubMed1989

A requirement for protein phosphorylation in regulating the meiotic and mitotic cell cycles in echinoderms.

Populations of hormone-stimulated starfish oocytes and fertilized sea urchin eggs undergo synchronous meiotic and mitotic divisions. We have studied the requirement for protein phosphorylation during these events by testing the effects of 6-dimethylaminopurine (6-DMAP) upon the incorporation of [32P]orthophosphate. It was found that 6-DMAP blocked meiosis reinitiation and early cleavage and simultaneously inhibited protein phosphorylation, without changing the rate of [35S]methionine incorporation or pattern of protein synthesis. The protein, cyclin (54 kDa in starfish and 57 kDa in sea urchin), continues to be synthesized in the presence of 6-DMAP. This protein is destroyed at first and second cell cycles when 6-DMAP is added 30 min following fertilization but not when this drug is present before fertilization. Thus, cyclin breakdown does not depend on the completion of the nuclear events of M-phase, and its time of breakdown is set at an early step between fertilization and first cleavage. Using tubulin immunostaining, we found that 6-DMAP did not affect the cortical microtubules and resting female centrioles of prophase-arrested starfish oocytes, whereas it induced a precocious disappearance of spindle fibers when applied to hormone-stimulated oocytes. While an early addition of 6-DMAP precluded nuclear breakdown and spindle formation in both systems, a late treatment always allowed chromosome separation and centriole separation. Under these conditions pericentriolar tubulin persisted and could organize new spindles after the inhibitor was removed. It is suggested that (1) the assembly of cortical and centriolar-associated microtubules is not controlled by the same factors as spindle-associated tubulin; (2) specific proteins which are required for the cell to enter the following M-phase can become operative only via a process depending upon protein phosphorylation; (3) microtubule-associated kinases may play an important role in MPF function and spindle dynamics.

Adenine↗