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Relevant bibliographies by topics / CDC2 Protein

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Academic literature on the topic 'CDC2 Protein'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "CDC2 Protein"

1

Burke, D. J., and D. Church. "Protein synthesis requirements for nuclear division, cytokinesis, and cell separation in Saccharomyces cerevisiae." Molecular and Cellular Biology 11, no. 7 (July 1991): 3691–98. http://dx.doi.org/10.1128/mcb.11.7.3691.

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Protein synthesis inhibitors have often been used to identify regulatory steps in cell division. We used cell division cycle mutants of the yeast Saccharomyces cerevisiae and two chemical inhibitors of translation to investigate the requirements for protein synthesis for completing landmark events after the G1 phase of the cell cycle. We show, using cdc2, cdc6, cdc7, cdc8, cdc17 (38 degrees C), and cdc21 (also named tmp1) mutants, that cells arrested in S phase complete DNA synthesis but cannot complete nuclear division if protein synthesis is inhibited. In contrast, we show, using cdc16, cdc17 (36 degrees C), cdc20, cdc23, and nocodazole treatment, that cells that arrest in the G2 stage complete nuclear division in the absence of protein synthesis. Protein synthesis is required late in the cell cycle to complete cytokinesis and cell separation. These studies show that there are requirements for protein synthesis in the cell cycle, after G1, that are restricted to two discrete intervals.

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Burke, D. J., and D. Church. "Protein synthesis requirements for nuclear division, cytokinesis, and cell separation in Saccharomyces cerevisiae." Molecular and Cellular Biology 11, no. 7 (July 1991): 3691–98. http://dx.doi.org/10.1128/mcb.11.7.3691-3698.1991.

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Protein synthesis inhibitors have often been used to identify regulatory steps in cell division. We used cell division cycle mutants of the yeast Saccharomyces cerevisiae and two chemical inhibitors of translation to investigate the requirements for protein synthesis for completing landmark events after the G1 phase of the cell cycle. We show, using cdc2, cdc6, cdc7, cdc8, cdc17 (38 degrees C), and cdc21 (also named tmp1) mutants, that cells arrested in S phase complete DNA synthesis but cannot complete nuclear division if protein synthesis is inhibited. In contrast, we show, using cdc16, cdc17 (36 degrees C), cdc20, cdc23, and nocodazole treatment, that cells that arrest in the G2 stage complete nuclear division in the absence of protein synthesis. Protein synthesis is required late in the cell cycle to complete cytokinesis and cell separation. These studies show that there are requirements for protein synthesis in the cell cycle, after G1, that are restricted to two discrete intervals.

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3

Molz, L., R. Booher, P. Young, and D. Beach. "cdc2 and the regulation of mitosis: six interacting mcs genes." Genetics 122, no. 4 (August 1, 1989): 773–82. http://dx.doi.org/10.1093/genetics/122.4.773.

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Abstract A cdc2-3w weel-50 double mutant of fission yeast displays a temperature-sensitive lethal phenotype that is associated with gross abnormalities of chromosome segregation and has been termed mitotic catastrophe. In order to identify new genetic elements that might interact with the cdc2 protein kinase in the regulation of mitosis, we have isolated revertants of the lethal double mutant. The suppressor mutations define six mcs genes (mcs: mitotic catastrophe suppressor) that are not allelic to any of the following mitotic control genes: cdc2, wee 1, cdc13, cdc25, suc1 or nim1. Each mcs mutation is recessive with respect to wild-type in its ability to suppress mitotic catastrophe. None confer a lethal phenotype as a single mutant but few of the mutants are expected to be nulls. A diverse range of genetic interactions between the mcs mutants and other mitotic regulators were uncovered, including the following examples. First, mcs2 cdc2w or mcs6 cdc2w double mutants display a cell cycle defect dependent on the specific wee allele of cdc2. Second, both mcs1 cdc25-22 or mcs4 cdc25-22 double mutants are nonconditionally lethal, even at a temperature normally permissive for cdc25-22. Finally, the characteristic suppression of the cdc25 phenotype by a loss-of-function wee1 mutation is reversed in a mcs3 mutant background. The mcs genes define new mitotic elements that might be activators or substrates of the cdc2 protein kinase.

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Okumura, E., T. Sekiai, S. Hisanaga, K. Tachibana, and T. Kishimoto. "Initial triggering of M-phase in starfish oocytes: a possible novel component of maturation-promoting factor besides cdc2 kinase." Journal of Cell Biology 132, no. 1 (January 1, 1996): 125–35. http://dx.doi.org/10.1083/jcb.132.1.125.

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G2-phase-arrested immature starfish oocytes contain inactive cdc2 kinase and cdc25 phosphatase, and an inactivator for cdc2 kinase. In this system, we have studied how the regulatory balance is apped toward the initial activation of cdc2 kinase. During the hormone-dependent period (Guerrier, P., and M. Doree, 1975. Dev. Biol. 47:341-348), p34cdc2 and cdc25 protein are already converted, though not fully, to active forms, whereas the inactivators for cdc2 kinase and cdc25 phosphatase are able to exhibit their activities if the hormone were removed. We produced "triggered oocytes," in which due to a neutralizing anticdc25 antibody, the activation of cdc2 kinase is prevented out cdc25 protein is phosphorylated slightly after the maturation-inducing hormonal stimulus. In contrast to control immature oocytes, in triggered oocytes the injected cdc2 kinase is not inactivated, and accordingly the level of cdc2 kinase activity required for meiosis reinitiation is much less. These results imply the presence of a cdc2 kinase activity-independent process(es) that suppresses the inactivator for cdc2 kinase and initially phosphorylates cdc25 protein, although this process is reversible during the initial activation of cdc2 kinase. At the most initial triggering of M-phase, the cdc2 kinase activity-independent process might trip the switch leading to the initial activation of cdc2 kinase. Thereafter, in parallel, the cdc2 kinase-dependent feedback loops described by others may cause further increase in cdc2 kinase activity. We propose that a putative suppressor, which downregulates the inactivator for cdc2 kinase independently of nuclear components, might be a previously unrecognized component of maturation-promoting factor.

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Margolis, Seth S., Jennifer A. Perry, Douglas H. Weitzel, Christopher D. Freel, Minoru Yoshida, Timothy A. Haystead, and Sally Kornbluth. "A Role for PP1 in the Cdc2/Cyclin B–mediated Positive Feedback Activation of Cdc25." Molecular Biology of the Cell 17, no. 4 (April 2006): 1779–89. http://dx.doi.org/10.1091/mbc.e05-08-0751.

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The Cdc25 phosphatase promotes entry into mitosis through the removal of inhibitory phosphorylations on the Cdc2 subunit of the Cdc2/CyclinB complex. During interphase, or after DNA damage, Cdc25 is suppressed by phosphorylation at Ser287 (Xenopus numbering; Ser216 of human Cdc25C) and subsequent binding of the small acidic protein, 14-3-3. As reported recently, at the time of mitotic entry, 14-3-3 protein is removed from Cdc25 and S287 is dephosphorylated by protein phosphatase 1 (PP1). After the initial activation of Cdc25 and consequent derepression of Cdc2/CyclinB, Cdc25 is further activated through a Cdc2-catalyzed positive feedback loop. Although the existence of such a loop has been appreciated for some time, the molecular mechanism for this activation has not been described. We report here that phosphorylation of S285 by Cdc2 greatly enhances recruitment of PP1 to Cdc25, thereby accelerating S287 dephosphorylation and mitotic entry. Moreover, we show that two other previously reported sites of Cdc2-catalyzed phosphorylation on Cdc25 are required for maximal biological activity of Cdc25, but they do not contribute to PP1 regulation and do not act solely through controlling S287 phosphorylation. Therefore, multiple mechanisms, including enhanced recruitment of PP1, are used to promote full activation of Cdc25 at the time of mitotic entry.

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Lopez-Girona, Antonia, Odile Mondesert, Janet Leatherwood, and Paul Russell. "Negative Regulation of Cdc18 DNA Replication Protein by Cdc2." Molecular Biology of the Cell 9, no. 1 (January 1998): 63–73. http://dx.doi.org/10.1091/mbc.9.1.63.

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Fission yeast Cdc18, a homologue of Cdc6 in budding yeast and metazoans, is periodically expressed during the S phase and required for activation of replication origins. Cdc18 overexpression induces DNA rereplication without mitosis, as does elimination of Cdc2-Cdc13 kinase during G2 phase. These findings suggest that illegitimate activation of origins may be prevented through inhibition of Cdc18 by Cdc2. Consistent with this hypothesis, we report that Cdc18 interacts with Cdc2 in association with Cdc13 and Cig2 B-type cyclins in vivo. Cdc18 is phosphorylated by the associated Cdc2 in vitro. Mutation of a single phosphorylation site, T104A, activates Cdc18 in the rereplication assay. The cdc18-K9 mutation is suppressed by a cig2 mutation, providing genetic evidence that Cdc2-Cig2 kinase inhibits Cdc18. Moreover, constitutive expression of Cig2 prevents rereplication in cells lacking Cdc13. These findings identify Cdc18 as a key target of Cdc2-Cdc13 and Cdc2-Cig2 kinases in the mechanism that limits chromosomal DNA replication to once per cell cycle.

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Booher, R., and D. Beach. "Site-specific mutagenesis of cdc2+, a cell cycle control gene of the fission yeast Schizosaccharomyces pombe." Molecular and Cellular Biology 6, no. 10 (October 1986): 3523–30. http://dx.doi.org/10.1128/mcb.6.10.3523.

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The cdc2+ gene of Schizosaccharomyces pombe is homologous to the CDC28 gene of Saccharomyces cerevisiae. Both genes share limited homology with vertebrate protein kinases and have protein kinase activity. cdc2+ has been subjected to mutagenesis in vitro. A null allele of the gene, constructed by insertion of the S. cerevisiae LEU2 gene into a site within the gene, has a phenotype similar to that of many temperature-sensitive alleles of cdc2. Mutations within the predicted ATP-binding site and in a region which may be a site of phosphorylation result in loss of cdc2+ activity. A single substitution of Gly-146 to Asp-146 has been identified in cdc2-1w, a dominant activated allele of the gene. The four introns within the cdc2+ gene have been deleted. The resulting gene not only functions in fission yeast but also rescues cdc28(Ts) strains of S. cerevisiae, a property which is not shared by the genomic cdc2+ gene.

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Booher, R., and D. Beach. "Site-specific mutagenesis of cdc2+, a cell cycle control gene of the fission yeast Schizosaccharomyces pombe." Molecular and Cellular Biology 6, no. 10 (October 1986): 3523–30. http://dx.doi.org/10.1128/mcb.6.10.3523-3530.1986.

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The cdc2+ gene of Schizosaccharomyces pombe is homologous to the CDC28 gene of Saccharomyces cerevisiae. Both genes share limited homology with vertebrate protein kinases and have protein kinase activity. cdc2+ has been subjected to mutagenesis in vitro. A null allele of the gene, constructed by insertion of the S. cerevisiae LEU2 gene into a site within the gene, has a phenotype similar to that of many temperature-sensitive alleles of cdc2. Mutations within the predicted ATP-binding site and in a region which may be a site of phosphorylation result in loss of cdc2+ activity. A single substitution of Gly-146 to Asp-146 has been identified in cdc2-1w, a dominant activated allele of the gene. The four introns within the cdc2+ gene have been deleted. The resulting gene not only functions in fission yeast but also rescues cdc28(Ts) strains of S. cerevisiae, a property which is not shared by the genomic cdc2+ gene.

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Sanchez, M., A. Calzada, and A. Bueno. "Functionally homologous DNA replication genes in fission and budding yeast." Journal of Cell Science 112, no. 14 (July 15, 1999): 2381–90. http://dx.doi.org/10.1242/jcs.112.14.2381.

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The cdc18(+) gene of the fission yeast Schizosaccharomyces pombe is involved in the initiation of DNA replication as well as in coupling the S phase to mitosis. In this work, we show that the Saccharomyces cerevisiae CDC6 gene complements cdc18-K46 ts and cdc18 deletion mutant S. pombe strains. The budding yeast gene suppresses both the initiation and the checkpoint defects associated with the lack of cdc18(+). The Cdc6 protein interacts in vivo with Cdc2 kinase complexes. Interestingly, Cdc6 is an in vitro substrate for Cdc13/Cdc2 and Cig1/Cdc2, but not for Cig2/Cdc2-associated kinases. Overexpression of Cdc6 in fission yeast induces multiple rounds of S-phase in the absence of mitosis and cell division. This CDC6-dependent continuous DNA synthesis phenotype is independent of the presence of a functional cdc18(+) gene product and, significantly, requires only Cig2/Cdc2-associated kinase activity. Finally, these S. pombe over-replicating cells do not require any protein synthesis other than that of Cdc6. Our data strongly suggest that CDC6 and cdc18(+) are functional homologues and also support the idea that controls restricting genome duplication diverge in fission and budding yeast.

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Yoon, H. J., S. Loo, and J. L. Campbell. "Regulation of Saccharomyces cerevisiae CDC7 function during the cell cycle." Molecular Biology of the Cell 4, no. 2 (February 1993): 195–208. http://dx.doi.org/10.1091/mbc.4.2.195.

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The yeast Cdc7 function is required for the G1/S transition and is dependent on passage through START, a point controlled by the Cdc28/cdc2/p34 protein kinase. CDC7 encodes a protein kinase activity, and we now show that this kinase activity varies in the cell cycle but that protein levels appear to remain constant. We present several lines of evidence that periodic activation of CDC7 kinase is at least in part through phosphorylation. First, the kinase activity of the Cdc7 protein is destroyed by dephosphorylation of the protein in vitro with phosphatase. Second, Cdc7 protein is hypophosphorylated and inactive as a kinase in extracts of cells arrested at START but becomes active and maximally phosphorylated subsequent to passage through START. The phosphorylation pattern of Cdc7 protein is complex. Phosphopeptide mapping reveals four phosphopeptides in Cdc7 prepared from asynchronous yeast cells. Both autophosphorylation and phosphorylation in trans appear to contribute to this pattern. Autophosphorylation is shown to occur by using a thermolabile Cdc7 protein. A protein in yeast extracts can phosphorylate and activate Cdc7 protein made in Escherichia coli, and phosphorylation is thermolabile in cdc28 mutant extracts. Cdc7 protein carrying a serine to alanine change in the consensus recognition site for Cdc28 kinase shows an altered phosphopeptide map, suggesting that this site is important in determining the overall Cdc7 phosphorylation pattern.

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Dissertations / Theses on the topic "CDC2 Protein"

1

Randall, Susan. "Interactions among the mitogen-activated protein kinase cascades and the identification of a novel cdc2-related protein kinase." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq29271.pdf.

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Potapova, Tamara. "Exploring mechanisms that control the activity of cyclin-dependent kinase 1 during mitotic transitions in somatic cells." Oklahoma City : [s.n.], 2009.

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Bhaduri, Samyabrata. "Regulation of CDK1 Activity during the G1/S Transition in S. cerevisiae through Specific Cyclin-Substrate Docking: A Dissertation." eScholarship@UMMS, 2014. http://escholarship.umassmed.edu/gsbs_diss/871.

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Several cell cycle events require specific forms of the cyclin-CDK complexes. It has been known for some time that cyclins not only contribute by activating the CDK but also by choosing substrates and/or specifying the location of the CDK holoenzyme. There are several examples of B-type cyclins identifying certain peptide motifs in their specific substrates through a conserved region in their structure. Such interactions were not known for the G1 class of cyclins, which are instrumental in helping the cell decide whether or not to commit to a new cell cycle, a function that is non-redundant with B-type cylins in budding yeast. In this dissertation, I have presented evidence that some G1 cyclins in budding yeast, Cln1/2, specifically identify substrates by interacting with a leucine-proline rich sequence different from the ones used by B-type cyclins. These “LP” type docking motifs determine cyclin specificity, promote phosphorylation of suboptimal CDK sites and multi-site phosphorylation of substrates both in vivo and in vitro. Subsequently, we have discovered the substrate-binding region in Cln2 and further showed that this region is highly conserved amongst a variety of fungal G1 cyclins from budding yeasts to molds and mushrooms, thus suggesting a conserved function across fungal evolution. Interestingly, this region is close to but not same as the one implicated in B-type cyclins to binding substrates. We discovered that the main effect of obliterating this interaction is to delay cell cycle entry in budding yeast, such that cells begin DNA replication and budding only at a larger than normal cell size, possibly resulting from incomplete multi-site phosphorylation of several key substrates. The docking-deficient Cln2 was also defective in promoting polarized bud morphogenesis. Quite interestingly, we found that a CDK inhibitor, Far1, could regulate the Cln2-CDK1 activity partly by inhibiting the Cln2-substrate interaction, thus demonstrating that docking interactions can be targets of regulation. Finally, by studying many fungal cyclins exogenously expressed in budding yeast, we discovered that some have the ability to make the CDK hyper-potent, which suggests that these cyclins confer special properties to the CDK. My work provides mechanistic clues for cyclinspecific events during the cell cycle, demonstrates the usefulness of synthetic strategies in problem solving and also possibly resolves long-standing uncertainties regarding functions of some cell cycle proteins.

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Kommajosyula, Naveen. "Regulation of DNA Replication Origins in Fission Yeast: A Dissertation." eScholarship@UMMS, 2009. https://escholarship.umassmed.edu/gsbs_diss/436.

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Cells need to complete DNA replication in a timely and error-free manner. To ensure that replication is completed efficiently and in a finite amount of time, cells regulate origin firing. To prevent any errors from being transmitted to the next generation, cells have the checkpoint mechanism. The S-phase DNA damage slows replication to allow the cell to repair the damage. The mechanism of replication slowing by the checkpoint was not clear in fission yeast, Schizosaccharomyces pombe, at the start of my thesis. The downstream targets of the DNA damage checkpoint in fission yeast were also unclear. I worked on identifying the downstream targets for the checkpoint by studying if Cdc25, a phosphatase, is a target of the checkpoint. Work from our lab has shown that origin firing is stochastic in fission yeast. Origins are also known to be inefficient. Inefficient origins firing stochastically would lead to large stretches of chromosome where no origins may fire randomly leading to long replication times, an issue called the random gap problem. However, cells do not take a long time to complete replication and the process of replication itself is efficient. I focused on understanding the mechanism by which cells complete replication and avoid the random gap problem by attempting to measure the firing efficiency of late origins. Genome-wide origin studies in fission yeast have identified several hundred origins. However, the resolution of these studies can be improved upon. I began a genome-wide origin mapping study using deep sequencing to identify origins at a greater resolution compared to the previous studies. We have extended our origin search to two other Schizosaccharomyces species- S. octosporus and S. japonicus.There have been no origin mapping studies on these fission yeasts and identifying origins in these species will advance the field of replication. My thesis research shows that Cdc25 is not a target of the S-phase DNA damage checkpoint. I showed that DNA damage checkpoint does not target Cdc2-Y15 to slow replication. Based on my preliminary observation, origin firing might be inhibited by the DNA damage checkpoint as a way to slow replication. My efforts to measure the firing efficiency of a late replicating sequence were hindered by potentially unidentified inefficient origins firing at a low rate and replicating the region being studied. Studying the origin efficiency was maybe further complicated by neighboring origins being able to passively replicate the region. To identify origins in recently sequenced Schizosaccharomyces species, we initiated the genome-wide origin mapping. The mapping was also done on S. pombe to identify inefficient origins not mapped by other mapping studies. My work shows that deep sequencing can be used to map origins in other species and provides a powerful tool for origin studies.

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Choi, Sung Hugh. "The Role of Dynamic Cdk1 Phosphorylation in Chromosome Segregation in Schizosaccharomyces pombe: A Dissertation." eScholarship@UMMS, 2010. https://escholarship.umassmed.edu/gsbs_diss/453.

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The proper transmission of genetic materials into progeny cells is crucial for maintenance of genetic integrity in eukaryotes and fundamental for reproduction of organisms. To achieve this goal, chromosomes must be attached to microtubules emanating from opposite poles in a bi-oriented manner at metaphase, and then should be separated equally through proper spindle elongation in anaphase. Failure to do so leads to aneuploidy, which is often associated with cancer. Despite the presence of a safety device called the spindle assembly checkpoint (SAC) to monitor chromosome bi-orientation, mammalian cells frequently possess merotelic kinetochore orientation, in which a single kinetochore binds microtubules emanating from both poles. Merotelically attached kinetochores escape from the surveillance mechanism of the SAC and when cells proceed to anaphase cause lagging chromosomes, which are a leading cause of aneuploidy in mammalian tissue cultured cells. The fission yeast monopolin complex functions in prevention of mal-orientation of kinetochores including merotelic attachments during mitosis. Despite the known importance of Cdk1 activity during mitosis, it has been unclear how oscillations in Cdk1 activity drive the dramatic changes in chromosome behavior and spindle dynamics that occur at the metaphase/anaphase transition. In two separate studies, we show how dynamic Cdk1 phosphorylation regulates chromosome segregation. First, we demonstrate that sequential phosphorylation and dephosphorylation of monopolin by Cdk1 and Cdc14 phosphatase respectively helps ensure the orderly execution of two discrete steps in mitosis, namely sister kinetochore bi-orientation at metaphase and spindle elongation in anaphase. Second, we show that elevated Cdk1 activity is crucial for correction of merotelic kinetochores produced in monopolin and heterochromatin mutants.

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Yassenko, Marina. "Modifications post-traductionnelles de la sous-unité régulatrice RIIα de la protéine kinase dépendante de l'AMP-cyclique au cours du cycle cellulaire." Paris 11, 2000. http://www.theses.fr/2000PA11T070.

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Dans les cellules de mammifères, les effets multiples de l'adénosine monophosphate cyclique (AMPc) sont assurés par l'intermédiaire de la protéine kinase dépendante de l'AMPc (PKA). Deux isoenzymes de la PKA, la PKA de type I et la PKA de type II, diffèrent selon la nature de leur sous-unités régulatrices (RI ou RII). Les modifications post-traductim:melles de ces isoformes majeures des sous-unités régulatrices RIα et RIIα de la PKA, majoritairement présentes dans les cellules HeLa, ont été étudiées au cours du cycle cellulaire. Des techniques de synchronisation cellulaire et le marquage par photoaffinité des sous-unités régulatrices de la PKA avec le 8-N3 [32P] AMPc ont été utilisés. Les deux résultats majeurs de cette étude sont : la mise en évidence d'une double phosphorylation de RIIα sur deux sites différents (par la sous-unité catalytique de la PKA et par une des kinases mitotiques (probablement p34cdc2), dans les cellules en mitose et la modification de l'activité de liaison à l'AMPc pour les deux isoformes RI et RII au cours de la transition G1/S. Ces deux effets se traduisent : 1) par un changement d'affinité de RIIα à la transition G2/M pour les AKAPs, protéines qui assurent sa localisation subcellulaire ; 2) par la modification du statut oxyditif de la cellule. Les processus oxydatifs par les radicaux libres des sous-unités régulatrices des PKAs, déjà mentionnés dans des maladies telles que le psoriasis, modifieraient l'activité PKA au cours du cycle cellulaire. L'étude présente met en évidence une régulation fine de l'activité des PKAs en fonction des modifications post-traductionnelles de leurs sous-unités régulatrices.

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Martino, Lisa. "Rôle et régulation de la kinase PLK-1 lors de l'entrée en mitose dans l'embryon de Caenorhabditis elegans." Thesis, Sorbonne Paris Cité, 2018. http://www.theses.fr/2018USPCC225.

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Lors de la division cellulaire, une cellule mère doit dupliquer (interphase) puis ségréger son matériel génétique de façon égale entre les deux cellules filles (mitose). Entre ces deux étapes, la cellule subit une réorganisation drastique gouvernée par l’acteur majeur Cdk1-Cycline B, conduisant à l’entrée en mitose. L’activation de cette kinase est régulée par une boucle d’auto-amplification où les premières molécules de Cdk1-Cycline B stimulent l’activation des suivantes. Il a été montré que la kinase Plk1 initie cette boucle d’auto-amplification en stimulant les activateurs et en réprimant les inhibiteurs de Cdk1-Cycline B en amont. Pour que cette kinase soit totalement active, elle doit être elle-même activée par Aurora A, en présence de son co-activateur Bora. Il est crucial de comprendre comment tous ces acteurs se coordonnent dans l’espace et dans le temps pour déclencher l’entrée en mitose car un dérèglement pourrait amener à une ségrégation de l’ADN anarchique, conduisant à la formation de tumeurs et l’apparition de cancers. Au cours de ma thèse, j’ai tout d’abord contribué à la mise en évidence d’un mécanisme conservé d’activation de Plk1 dans les cellules humaines et chez C. elegans (PLK-1), impliquant le co-activateur Bora ou SPAT-1 chez C. elegans. Nous avons montré que la phosphorylation de SPAT-1 par Cdk1-Cycline B induit son interaction avec PLK-1, ce qui promeut la phosphorylation de PLK-1 par Aurora A et donc son activation in vitro. Ce mécanisme phospho-dépendant de SPAT-1 est important in vivo pour contrôler dans le temps l’entrée en mitose. De plus, l’activation de Plk1 in vitro avec les protéines humaines suggèrent fortement une conservation du mécanisme. Nous avons ensuite montré que la phosphorylation de Bora et de SPAT-1 par Cdk1 sur les résidus S41, S112, S137 et S119, S190, T229 respectivement, est nécessaire à leur interaction avec Plk1/PLK-1, déclenchant ensuite l’activation de Plk1/PLK-1 et l’entrée en mitose. Ces résultats démontrent que Bora/SPAT-1 phosphorylée fait partie de la boucle d’auto-amplification de Cdk1-Cycline B via l’activation de Plk1, permettant à terme d’activer de façon irréversible les acteurs de l’entrée en mitose. Par la suite, je me suis focalisée sur le rôle de PLK-1 dans la rupture de l’enveloppe nucléaire en utilisant l’embryon de C. elegans comme système modèle. Après avoir démontré que PLK-1 est cruciale pour la rupture de l’enveloppe nucléaire dans les embryons, j’ai observé une localisation de PLK-1 à l’enveloppe nucléaire avant sa rupture et j’ai identifié un complexe de nucléoporines impliqué dans ce processus. En effet, NPP-1, NPP-4 et NPP-11 dont la fonction est de réguler le transport nucléo-cytoplasmique, ont également un second rôle dans le recrutement de PLK-1 aux pores nucléaires. PLK-1 interagit avec ses substrats phosphorylés par deux types de mécanismes d’amorçage Plk1-dépendant et indépendant, impliquant une autre kinase en amont comme Cdk1-Cycline B par exemple. J’ai montré que le recrutement de PLK-1 aux pores dépend des deux mécanismes, nécessitant donc une coordination entre Cdk1-Cycline B et PLK-1. Une fois que PLK-1 est au centre du pore nucléaire, elle peut alors probablement phosphoryler de nombreuses nucléoporines et participer au désassemblage des pores, conduisant à la rupture de l’enveloppe nucléaire
During cell division, a mother cell duplicates (interphase) and then segregate its genetic material equally between the two daughter cells (mitosis). Between these two stages, the cell undergoes a drastic reorganization governed by the major actor Cdk1-Cyclin B, leading to mitotic entry. The activation of this kinase is regulated by an auto-amplification loop where the first molecules of Cdk1-Cyclin B stimulate activation of the following. Plk1 kinase has been shown to initiate this self-amplification loop by stimulating activators and repressing upstream Cdk1-Cyclin B inhibitors. For this kinase to be fully active, it must itself be activated by Aurora A, in the presence of its coactivator Bora. It is crucial to understand how all these actors coordinate in space and time to trigger mitotic entry because a disruption could lead to a segregation of anarchic DNA, leading to the formation of tumors and the appearance of cancers. During my thesis, I first contributed to demonstrate a conserved mechanism of Plk1 activation in human cells and in C. elegans (PLK-1), involving the coactivator Bora or SPAT-1 in C. elegans. We have shown that the phosphorylation of SPAT-1 by Cdk1-Cyclin B induces its interaction with PLK-1, which promotes the phosphorylation of PLK-1 by Aurora A and thus its activation in vitro. This phosphory-dependent mechanism of SPAT-1 is important in vivo for controlling the entry into mitosis over time. In addition, activation of Plk1 in vitro with human proteins strongly suggests conservation of the mechanism. We then showed that the phosphorylation of Bora and SPAT-1 by Cdk1 on residues S41, S112, S137 and S119, S190, T229 respectively, is necessary for their interaction with Plk1 / PLK-1, then triggering the activation of Plk1 / PLK-1 and mitotic entry. These results demonstrate that phosphorylated Bora / SPAT-1 is part of the self-amplification loop of Cdk1-Cyclin B via the activation of Plk1, ultimately enabling irreversible activation of the actors of mitotic entry. Subsequently, I focused on the role of PLK-1 in nuclear envelope breakdown using the C. elegans early embryo as a model system. After demonstrating that PLK-1 is crucial for the nuclear envelope breakdown in embryos, I observed a localization of PLK-1 to the nuclear envelope before its rupture and I identified a nucleoporin complex involved in this process. Indeed, NPP-1, NPP-4 and NPP-11 whose function is to regulate nucleo-cytoplasmic transport, also have a second role in the recruitment of PLK-1 to nuclear pores. PLK-1 interacts with its phosphorylated substrates by two types of Plk1-dependent and independent priming mechanisms, involving another upstream kinase such as Cdk1-Cyclin B for example. I have shown that the recruitment of PLK-1 to the pores depends on both mechanisms, thus requiring coordination between Cdk1-Cyclin B and PLK-1. Once PLK-1 is at the center of the nuclear pore, it can probably phosphorylate many nucleoporins and participate in the disassembly of pores, leading to tnuclear envelope breakdown

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8

Borysov, Sergiy I. "B-Raf is an essential component of the mitotic machinery critical for activation of MAPK signaling during mitosis in Xenopus egg extracts." [Tampa, Fla] : University of South Florida, 2006. http://purl.fcla.edu/usf/dc/et/SFE0001759.

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Anscombe, Elizabeth. "Targeting protein-protein interactions for cancer therapy." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:6155f526-5e56-454c-819d-9510fb6f9e02.

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Protein-protein interactions (PPIs) are key drug targets and recent breakthroughs in this area are providing insight into the types of molecules needed to selectively and potently inhibit a target traditionally seen as untractable. The rules that have been used to design classic substratecompetitive drugs (for example Lipinski's rule of five) may not apply in this new field in the same way. Here I present work performed in three systems that are well-validated drug targets for oncogenesis: the CDK2/cyclin A complex, the PLK1 Polobox domain and MDM2. In each case the site of the protein-protein interaction is defined and understood and the rationale for pharmaceutical intervention is clear. I use these as a model system to evaluate the characteristics of drugs that target protein-protein interaction sites and present work on the development of inhibitors as potential leads for subsequent drug development. In Chapter 1 I introduce the problems, challenges and rewards of PPI drug development; in Chapter 2 I present co-crystal structures of MDM2 with isoindolinone inhibitors; in Chapter 3 I detail attempts to co-crystallise the Plk1 Polobox with inhibitors and screen potential inhibitors; in Chapter 4 I present the results of screening to identify inhibitors of Cyclin A recruitment; and in Chapter 5 I discuss other strategies for inhibition of the CDK2/cyclin A complex, including results with a covalent inhibitor. Through these projects I have been able to demonstrate the wide applicability of the PPI inhibition approach, identify key features of drugs able to inhibit PPIs and contribute to drug design in each system.

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10

LEBEL-BINAY, SOPHIE. "Caracterisation fonctionnelle d'une nouvelle proteine transmembranaire : cd82." Paris 7, 1995. http://www.theses.fr/1995PA077277.

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La glycoproteine cd82 a ete identifiee et clonee dans notre laboratoire pour son expression preferentielle sur les lignees cellulaires sensibles a la lyse par les effecteurs nk/lak. Cette molecule de 267 acides amines (35 a 100 kda) est une proteine de type iii avec 4 segments transmembranaires, des extremites nh2 et cooh intracytoplasmiques et un grand domaine extracellulaire. Elle appartient a la famille des proteines tetra span transmembranaires (tst) qui comprend cd9, cd37, cd53, cd63 et cd81. Cd82. Elle est exprimee a la surface de nombreux types cellulaires. Son expression est augmentee apres activation ou differenciation des cellules mononuclees (lymphocytes, monocytes). Cd82 possede des proprietes de transduction sur la lignee monocytaire u937 (mobilisation de calcium intracellulaire). Cd82 est une molecule de costimulation de l'activation des lymphocytes t. Les lymphocytes t stimules in vitro par des acs anti-cd3 et anti-cd82 immobilises, se differencient et produisent de l'il-2 et de l'ifng

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Books on the topic "CDC2 Protein"

1

Randall, Susan. Interactions among the mitogen-activated protein kinase cascades and the identification of a novel cdc2-related protein kinase. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1999.

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White, Anne Marie. Regulation of Cdc7 protein kinase activity by phosphorylation. Manchester: University of Manchester, 1994.

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Chen, Luping. Murine CDC25-related proteins: Activators of Ras. Ottawa: National Library of Canada, 1993.

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Anderluh, Gregor, and Robert Gilbert, eds. MACPF/CDC Proteins - Agents of Defence, Attack and Invasion. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8881-6.

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NKIAMRE: A novel conserved cdc2-related kinase with features of both mitogen-activated protein kinases and cyclin-dependent kinases. Ottawa: National Library of Canada, 2002.

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Pontus, Aspenstrøm, ed. The pombe Cdc 15 homology proteins. Austin, Tex: Landes Bioscience, 2009.

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Gilbert, Robert, and Gregor Anderluh. MACPF/CDC Proteins - Agents of Defence, Attack and Invasion. Springer, 2016.

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Gilbert, Robert, and Gregor Anderluh. MACPF/CDC Proteins - Agents of Defence, Attack and Invasion. Ingramcontent, 2014.

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Maruta, Hiroshi. PAKs, RAC/CDC42 -Activated Kinases: Towards the Cure of Cancer and Other PAK-Dependent Diseases. Elsevier Science & Technology Books, 2013.

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B, Kastan M., and Imperial Cancer Research Fund (Great Britain), eds. Checkpoint controls and cancer. Plainview, NY: Cold Spring Harbor Laboratory Press, 1997.

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Book chapters on the topic "CDC2 Protein"

1

Marcote, M. Jesús, Michele Pagano, and Giulio Draetta. "Cdc2 Protein Kinase: Structure-Function Relationships." In Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle, 30–49. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514320.ch4.

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Draetta, Giulio. "Biochemical Regulation of the CDC2 Protein Kinase." In Cellular Regulation by Protein Phosphorylation, 363–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75142-4_46.

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Nigg, E. A., W. Krek, and P. Gallant. "Regulation of the Mitotic CDC2 Protein Kinase." In DNA Replication and the Cell Cycle, 147–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77040-1_11.

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Vogel, Lee, and Blandine Baratte. "Suc1: cdc2 affinity reagent or essential cdk adaptor protein?" In Progress in Cell Cycle Research, 129–35. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5873-6_13.

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Gabrielli, Brian, and Andrew Burgess. "Cdc25 Family Phosphatases in Cancer." In Protein Tyrosine Phosphatases in Cancer, 283–306. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3649-6_11.

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Bell, Stephen D. "Archaeal Orc1/Cdc6 Proteins." In Subcellular Biochemistry, 59–69. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-4572-8_4.

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Medway, Christopher, and Kevin Morgan. "CD2-Associated Protein (CD2AP)." In Genetic Variants in Alzheimer's Disease, 201–8. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7309-1_11.

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Anderluh, Gregor, Matic Kisovec, Nada Kraševec, and Robert J. C. Gilbert. "Distribution of MACPF/CDC Proteins." In MACPF/CDC Proteins - Agents of Defence, Attack and Invasion, 7–30. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8881-6_2.

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Taylor, Lacey D., and David E. Nelson. "Chlamydial MACPF Protein CT153." In MACPF/CDC Proteins - Agents of Defence, Attack and Invasion, 255–69. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8881-6_13.

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Ota, Katja, Matej Butala, Gabriella Viero, Mauro Dalla Serra, Kristina Sepčić, and Peter Maček. "Fungal MACPF-Like Proteins and Aegerolysins: Bi-component Pore-Forming Proteins?" In MACPF/CDC Proteins - Agents of Defence, Attack and Invasion, 271–91. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8881-6_14.

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Conference papers on the topic "CDC2 Protein"

1

Lopes, Ana P., Joel van Roon, Sofie Blokland, Maojie Wang, Eleni Chouri, Aike A. Kruize, Boudewijn Burgering, Marzia Rossato, Timothy R. Radstake, and Maarten Hillen. "AB0176 MITOGEN- AND STRESS-ACTIVATED PROTEIN KINASE-1 (MSK1) AS THE LINK BETWEEN MIR-130A-DYSREGULATION AND CDC2-ACTIVATION IN SJöGREN’S SYNDROME." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.6806.

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Hua, Kuo-Tai, Ching-Ting Tan, Chi-Kuan Chen, Min-Wei Chen, Michael Hsiao, and Min-Liang Kuo. "Abstract 3422: N-α-acetyltransferase 10 protein suppresses cancer cell metastasis by binding PIX proteins and inhibiting Cdc42/Rac1 activity." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3422.

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Hua, Kuo-Tai, Michael Hsiao, and Min-Liang Kuo. "Abstract 3376: Human arrest defective 1 protein suppresses cancer cell metastasis by binding PIX/Cool proteins and inhibiting Cdc42/Rac1 activity." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3376.

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Hu, Shanhu, Alexey V. Danilov, Kristina M. Godek, Bernardo Orr, Laura J. Tafe, Vincent A. Memoli, Fabrizio Galimberti, et al. "Abstract 4549: CDK2 inhibition causes anaphase catastrophe through the centrosomal protein CP110." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4549.

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Koshkina, Nadezhda V., Ge Yang, and Eugenie S. Kleinerman. "Abstract 5115: The role of Cdc42-interacting protein 4 (CIP4) in osteosarcoma tumorigenesis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5115.

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Takehito Azuma, Hisao Moriya, Hayato Matsumuro, and Hiroaki Kitano. "A robustness analysis of eukaryotic cell cycle concerning Cdc25 and wee1 proteins." In 2006 IEEE Conference on Computer Aided Control System Design, 2006 IEEE International Conference on Control Applications, 2006 IEEE International Symposium on Intelligent Control. IEEE, 2006. http://dx.doi.org/10.1109/cacsd-cca-isic.2006.4776903.

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Azuma, Takehito, Hisao Moriya, Hayato Matsumuro, and Hiroaki Kitano. "A Robustness Analysis of Eukaryotic Cell Cycle concerning Cdc25 and Wee1 Proteins." In 2006 IEEE International Conference on Control Applications. IEEE, 2006. http://dx.doi.org/10.1109/cca.2006.286135.

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Nath, Somsubhra, Taraswi Banerjee, Debrup Sen, Tania Das, and Susanta Roychoudhury. "Abstract 3075: A novel transcriptional role of spindle assembly checkpoint protein Cdc20 regulating the expression of mitotic ubiquitin carrier protein UbcH10." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3075.

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Kshama Goyal and M. Vidyasagar. "Predicting protein-protein interactions in E. coli using machine learning methods." In 2007 46th IEEE Conference on Decision and Control. IEEE, 2007. http://dx.doi.org/10.1109/cdc.2007.4434364.

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Siripornadulsil, Surasak, and Wilailak Siripornadulsil. "Characterization of Cadmium-Resistant Bacteria and Their Application for Cadmium Bioremediation." In ASME 2009 12th International Conference on Environmental Remediation and Radioactive Waste Management. ASMEDC, 2009. http://dx.doi.org/10.1115/icem2009-16072.

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Abstract:

On a global basis, trace-metal pollution is one of the most pervasive environmental problems. It is particularly difficult to prevent or clean up because the metals are toxic in their elemental form and cannot be decomposed. Bioremediation has been shown to be a powerful system for heavy metal pollution clean up and prevention. In this work, we characterized the cadmium (Cd)-resistant bacteria isolated from rice field soil downstream from zinc (Zn) mineralized area which the owners were contaminated at high level of cadmium content in their blood (>10 μgCd/g creatinine). We found that all 24 isolated bacteria tolerated toxic Cd concentrations (2,500 μM). In order to determine whether the Cd toxicity affected the growth of isolated bacteria, we grew the isolated bacterial cells in the absence and presence of toxic concentrations of CdCl2 (500 μM). In the absence of Cd, all isolated bacterial cells grew slightly better than in the presence of toxic concentrations of Cd. In addition, the Cd binding capacity of all isolated bacteria were very high, ranging from 6.38 to 9.38 log[Cd(atom)]/cell when grown in the presence of 500 μM CdCl2. Furthermore, the stability of Cd-bacteria complex of all isolated bacteria was affected by 1mM EDTA. When grown in the presence of 500 μM CdCl2, Cd-resistant isolates S2500-6, -8, -9, -15, -17, -18, -19, and -22 increasingly produced proteins containing cysteine (SH-group) (from 1.3 to 2.2 times) as well as 11 isolates of Cd-resistant bacteria, including S2500-1, -2, -3, -5, -6, -8, -9, -11, -16, -20, and -21, increasingly produced inorganic sulfide (1.5 to 4.7 times). Furthermore, the Sulfur K-edge X-ray absorption near-edge structure (XANES) spectroscopy studies indicated that Cd-resistant isolated S2500-3 precipitated amounts of cadmium sulfide (CdS), when grown in the presence of 500 μM CdCl2. The results suggested that these Cd-resistant bacteria have potential ability to precipitate a toxic soluble CdCl2 as nontoxic insoluble CdS. Interestingly, Cd-resistant bacteria isolated S2500-3, -8, -9,and -20 increased cadmium tolerance of Thai jasmine rice (Kao Hom Mali 105) when grown in the presence of 200 μM CdCl2. These 4 isolates also decreased cadmium concentration accumulation in Kao Hom Mali 105 plant at 61, 9, 6, and 17%, respectively when grown in the presence of 200 μM CdCl2. They were identified by 16S rDNA sequence analysis and classified as Cupriavidus taiwanensis (isolate S2500-3) and Pseudomonas aeruginosa (isolates S2500-8, -9, and -20).

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