cdc2 is a component of the M phase-specific histone H1 kinase: Evidence for identity with MPF

Arion, Dominique; Meijer, Laurent; Brizuela, Leonardo; Beach, David

doi:10.1016/0092-8674(88)90060-8

Cited by 520 publications

(206 citation statements)

References 47 publications

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“…Interestingly, the conversion of Sp histones to their modified form in vivo takes place in eggs treated with DMAP, indicating that the sperm histone kinase is DMAPinsensitive (41). The sperm histone kinase is thus likely to be distinct from the mitotic histone kinase p34 cdc2 (44) and from PKC, which are both inhibited by DMAP (45) (this study).…”

Section: Pkc-mediated Interphase Laminmentioning

confidence: 96%

Protein Kinase C-mediated Interphase Lamin B Phosphorylation and Solubilization

Collas¹,

Thompson²,

Fields³

et al. 1997

Journal of Biological Chemistry

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Disassembly of the sperm nuclear envelope at fertilization is one of the earliest events in the development of the male pronucleus. We report that nuclear lamina disassembly in interphase sea urchin egg cytosol is a result of lamin B phosphorylation mediated by protein kinase C (PKC). Lamin B of permeabilized sea urchin sperm nuclei incubated in fertilized egg G 1 phase cytosolic extract is phosphorylated within 1 min of incubation and solubilized prior to sperm chromatin decondensation. Phosphorylation is Ca 2؉ -dependent. It is reversibly inhibited by the PKC-specific inhibitor chelerythrine, a PKC pseudosubstrate inhibitor peptide, and a PKC substrate peptide, but not by inhibitors of PKA, p34 cdc2 or calmodulin kinase II. Phosphorylation is inhibited by immunodepletion of cytosolic PKC and restored by addition of purified rat brain PKC. Sperm lamin B is a substrate for rat brain PKC in vitro, resulting in lamin B solubilization. Two-dimensional phosphopeptide maps of lamin B phosphorylated by the cytosolic kinase and by purified rat PKC are virtually identical. These data suggest that PKC is the major kinase required for interphase disassembly of the sperm lamina.The nuclear lamina consists of a polymeric network of intermediate filament molecules, the nuclear lamins, underlying the inner nuclear membrane. The lamina is a dynamic structure, undergoing expansion during interphase of the cell cycle, and depolymerization at mitosis upon breakdown of the nuclear envelope (NE) 1 (1). Mitotic disassembly and reassembly of the lamina is regulated by reversible lamin phosphorylation and dephosphorylation (1). Interphase lamin phosphorylation has also been reported (2-6), but its significance is not fully understood.Several lamin kinases have been identified that promote mitotic lamina solubilization or inhibit lamina assembly in vitro. They include cyclin B/p34 cdc2 (7), S6 kinase II (8), protein kinase C (PKC) (4, 9), and the cAMP-dependent protein kinase PKA (10). Down-regulation of PKA has also been shown to be essential for mitotic lamina disassembly (11). Although not a lamin kinase, Ca 2ϩ /calmodulin-dependent kinase II (CaM kinase II) is also involved in mitotic NE breakdown in sea urchin embryos (12). PKC has also been shown to phosphorylate chicken lamin B 2 in interphase, a process thought to regulate lamin import into the nucleus (13). These observations imply that multiple kinases regulate the dynamics of the nuclear lamina during the cell cycle. The transformation of the sea urchin sperm nucleus into a pronucleus at fertilization provides an opportunity to investigate NE assembly/disassembly during interphase. Sea urchin eggs are fertilized in G 1 phase of the first cell cycle after completion of both meiotic divisions. At fertilization, the sperm NE vesiculates and a new NE reforms around the male pronucleus as the sperm chromatin decondenses (14). Male pronuclear formation has been duplicated in a cell-free system by incubating detergent-permeabilized sperm nuclei in fertilized egg extracts (15)(16)(1...

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Section: Pkc-mediated Interphase Laminmentioning

confidence: 96%

Protein Kinase C-mediated Interphase Lamin B Phosphorylation and Solubilization

Collas¹,

Thompson²,

Fields³

et al. 1997

Journal of Biological Chemistry

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“…It is constituted in part by a protein of 34 kDa, which shares H1 kinase activity and is related to the product of the gene cdc2 controlling the cell division in the yeast, Schizosaccharomyces pombe [2][3][4][5].…”

Section: Introductionmentioning

confidence: 99%

A purified complex from Xenopus oocytes contains a p47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF‐1γ and EF‐1β

et al. 1989

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A high molecular mass complex isolated from Xenopus laevis oocytes contains three main proteins, respectively p30, p36 and p47. The p47 protein has been reported to be an in vivo substrate of the cell division control protein kinase p34 '~2. From polypeptide sequencing, we now show that the p30 and the p47 correspond to elongation factor EF-lfl and EF-ly.Furthermore, the p30 and p36 proteins were phosphorylated in vitro by casein kinase II.

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“…Des études ont montré que CDK1, -2, -5, -7 et -9 sont les protéine kinases les plus sensibles à la molécule [8]. Ainsi, exploitée par la société Cyclacel (Berkeley Heights, New Jersey, États-Unis) sous le nom de Seliciclib ou CYC202, elle a notamment atteint la phase 2 d'études cliniques pour le traitement du cancer du poumon non à petites cellules et, plus récemment, de la maladie de Cushing, dont les résultats sont attendus en 2017 4 . La rosco-2 L'article décrivant son activité inhibitrice est cité plus de 875 fois (source Web of Sciences TM ).…”

Section: Synthèse Revuesunclassified

“…3 L'estimation des cibles affectées par l'inhibiteur a été la plus exhaustive possible. 4 www.clinicaltrial.gov, NCT00372073 et NCT02160730. significatives d'enzymes natives, rendant ainsi possibles des approches à grande échelle, telles que le criblage moléculaire [5].…”

Section: Synthèse Revuesunclassified