Journal articles: 'Cyclin-dependent kinases'

1

Sclafani, Robert A. "Cyclin dependent kinase activating kinases." Current Opinion in Cell Biology 8, no. 6 (December 1996): 788–94. http://dx.doi.org/10.1016/s0955-0674(96)80079-2.

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Gitig, Diana M., and Andrew Koff. "Cdk Pathway: Cyclin-Dependent Kinases and Cyclin-Dependent Kinase Inhibitors." Molecular Biotechnology 19, no. 2 (2001): 179–88. http://dx.doi.org/10.1385/mb:19:2:179.

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3

Malumbres, Marcos. "Cyclin-dependent kinases." Genome Biology 15, no. 6 (2014): 122. http://dx.doi.org/10.1186/gb4184.

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4

Harper, J. W., and P. D. Adams. "Cyclin-Dependent Kinases." Chemical Reviews 101, no. 8 (August 2001): 2511–26. http://dx.doi.org/10.1021/cr0001030.

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5

Dynlacht, B. D., K. Moberg, J. A. Lees, E. Harlow, and L. Zhu. "Specific regulation of E2F family members by cyclin-dependent kinases." Molecular and Cellular Biology 17, no. 7 (July 1997): 3867–75. http://dx.doi.org/10.1128/mcb.17.7.3867.

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The transcription factor E2F-1 interacts stably with cyclin A via a small domain near its amino terminus and is negatively regulated by the cyclin A-dependent kinases. Thus, the activities of E2F, a family of transcription factors involved in cell proliferation, are regulated by at least two types of cell growth regulators: the retinoblastoma protein family and the cyclin-dependent kinase family. To investigate further the regulation of E2F by cyclin-dependent kinases, we have extended our studies to include additional cyclins and E2F family members. Using purified components in an in vitro system, we show that the E2F-1-DP-1 heterodimer, the functionally active form of the E2F activity, is not a substrate for the active cyclin D-dependent kinases but is efficiently phosphorylated by the cyclin B-dependent kinases, which do not form stable complexes with the E2F-1-DP-1 heterodimer. Phosphorylation of the E2F-1-DP-1 heterodimer by cyclin B-dependent kinases, however, did not result in down-regulation of its DNA-binding activity, as is readily seen after phosphorylation by cyclin A-dependent kinases, suggesting that phosphorylation per se is not sufficient to regulate E2F DNA-binding activity. Furthermore, heterodimers containing E2F-4, a family member lacking the cyclin A binding domain found in E2F-1, are not efficiently phosphorylated or functionally down-regulated by cyclin A-dependent kinases. However, addition of the E2F-1 cyclin A binding domain to E2F-4 conferred cyclin A-dependent kinase-mediated down-regulation of the E2F-4-DP-1 heterodimer. Thus, both enzymatic phosphorylation and stable physical interaction are necessary for the specific regulation of E2F family members by cyclin-dependent kinases.

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Malumbres, Marcos, and Mariano Barbacid. "Mammalian cyclin-dependent kinases." Trends in Biochemical Sciences 30, no. 11 (November 2005): 630–41. http://dx.doi.org/10.1016/j.tibs.2005.09.005.

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7

Clarke, Paul R. "Cyclin-Dependent Kinases: CAK-handed kinase activation." Current Biology 5, no. 1 (January 1995): 40–42. http://dx.doi.org/10.1016/s0960-9822(95)00013-3.

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8

Feroche, Alemu Tadesse, and Frehiwot Beyene Woselassie. "A review on macrocyclic kinase inhibitors in clinical trials." International Journal of Pharmaceutical Chemistry and Analysis 11, no. 2 (July 15, 2024): 147–52. http://dx.doi.org/10.18231/j.ijpca.2024.020.

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Macrocyclic kinase inhibitors have high binding affinity and selectivity towards a variety of kinases including mammalian target of rapamycin complex 1/2, janus kinases/ Fms like tyrosine kinase, cyclin-dependent kinases and anaplastic lymphoma kinase1. Recently, few macrocyclic kinase inhibitors have entered clinical trial for treatment different types of cancers including leukemia, non-small cell lung cancer, myelofibrosis, breast cancer, glioblastoma and lymphoma. Of them, ridaforomilus has completed Phase III clinical trial and is waiting to be approved for treatment of breast cancer and advanced leukemia. Pacritinib is also currently being tested in phase III clinical trial for treatment of myelofibrosis and, loratinib is being evaluated for advanced ALK gene positive nonsmall cell lung carcinoma. The broad-spectrum cyclin-dependent kinases inhibitor, TGO2, has also entered phase II clinical trial for treatment of glioblastoma and advanced leukemia.

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9

Wang, Fuhu, Dale Corbett, Hitoshi Osuga, Sachiko Osuga, Joh-E. Ikeda, Ruth S. Slack, Matthew J. Hogan, Antoine M. Hakim, and David S. Park. "Inhibition of Cyclin-Dependent Kinases Improves CA1 Neuronal Survival and Behavioral Performance after Global Ischemia in the Rat." Journal of Cerebral Blood Flow & Metabolism 22, no. 2 (February 2002): 171–82. http://dx.doi.org/10.1097/00004647-200202000-00005.

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Increasing evidence suggests that cyclin-dependent kinases participate in neuronal death induced by multiple stresses in vitro. However, their role in cell death paradigms in vivo is not well characterized. Accordingly, the authors examined whether cyclin-dependent kinase inhibition resulted in functionally relevant and sustained neuroprotection in a model of global ischemia. Intracerebroventricular administration of the cyclin-dependent kinase inhibitor flavopiridol, immediately or at 4 hours postreperfusion after a global insult, reduced injury in the CA1 of the hippocampus when examined 7 days after reperfusion. No significant protection was observed when flavopiridol was administered 8 hours after reperfusion. The tumor-suppressor retinoblastoma protein, a substrate of cyclin-dependent kinase, was phosphorylated on a cyclin-dependent kinase consensus site after the global insult; this phosphorylation was inhibited by flavopiridol administration. Importantly, flavopiridol had no effect on core body temperature, suggesting that the mechanism of neuroprotection was through cyclin-dependent kinase inhibition but not through hypothermia. Furthermore, inhibition of cyclin-dependent kinases improved spatial learning behavior as assessed by the Morris water maze 7 to 9 days after reperfusion. However, the histologic protection observed at day 7 was absent 28 days after reperfusion. These results indicate that cyclin-dependent kinase inhibition provides an extended period of morphologic and functional neuroprotection that may allow time for other neuroprotective modalities to be introduced.

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Canavese, Miriam, Loredana Santo, and Noopur Raje. "Cyclin dependent kinases in cancer." Cancer Biology & Therapy 13, no. 7 (May 2012): 451–57. http://dx.doi.org/10.4161/cbt.19589.

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11

Park, David S., Fuhu Wang, and Michael J. O’Hare. "Cyclin-dependent kinases and stroke." Expert Opinion on Therapeutic Targets 5, no. 5 (October 2001): 557–67. http://dx.doi.org/10.1517/14728222.5.5.557.

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12

Harper, J. W., and P. D. Adams. "ChemInform Abstract: Cyclin-Dependent Kinases." ChemInform 32, no. 41 (May 24, 2010): no. http://dx.doi.org/10.1002/chin.200141284.

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13

Grison, Alice, and Suzana Atanasoski. "Cyclins, Cyclin-Dependent Kinases, and Cyclin-Dependent Kinase Inhibitors in the Mouse Nervous System." Molecular Neurobiology 57, no. 7 (June 6, 2020): 3206–18. http://dx.doi.org/10.1007/s12035-020-01958-7.

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14

Jiang, Hong, Hubert S. Chou, and Liang Zhu. "Requirement of Cyclin E-Cdk2 Inhibition in p16INK4a-Mediated Growth Suppression." Molecular and Cellular Biology 18, no. 9 (September 1, 1998): 5284–90. http://dx.doi.org/10.1128/mcb.18.9.5284.

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ABSTRACT Loss-of-function mutations of p16 INK4a have been identified in a large number of human tumors. An established biochemical function of p16 is its ability to specifically inhibit cyclin D-dependent kinases in vitro, and this inhibition is believed to be the cause of the p16-mediated G1 cell cycle arrest after reintroduction of p16 into p16-deficient tumor cells. However, a mutant of Cdk4, Cdk4N158, designed to specifically inhibit cyclin D-dependent kinases through dominant negative interference, was unable to arrest the cell cycle of the same cells (S. van den Heuvel and E. Harlow, Science 262:2050–2054, 1993). In this study, we determined functional differences between p16 and Cdk4N158. We show that p16 and Cdk4N158 inhibit the kinase activity of cellular cyclin D1 complexes through different mechanisms. p16 dissociated cyclin D1-Cdk4 complexes with the release of bound p27 KIP1 , while Cdk4N158 formed complexes with cyclin D1 and p27. In cells induced to overexpress p16, a higher portion of cellular p27 formed complexes with cyclin E-Cdk2, and Cdk2-associated kinase activities were correspondingly inhibited. Cells engineered to express moderately elevated levels of cyclin E became resistant to p16-mediated growth suppression. These results demonstrate that inhibition of cyclin D-dependent kinase activity may not be sufficient to cause G1 arrest in actively proliferating tumor cells. Inhibition of cyclin E-dependent kinases is required in p16-mediated growth suppression.

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15

Harper, J. W., S. J. Elledge, K. Keyomarsi, B. Dynlacht, L. H. Tsai, P. Zhang, S. Dobrowolski, C. Bai, L. Connell-Crowley, and E. Swindell. "Inhibition of cyclin-dependent kinases by p21." Molecular Biology of the Cell 6, no. 4 (April 1995): 387–400. http://dx.doi.org/10.1091/mbc.6.4.387.

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p21Cip1 is a cyclin-dependent kinase (Cdk) inhibitor that is transcriptionally activated by p53 in response to DNA damage. We have explored the interaction of p21 with the currently known Cdks. p21 effectively inhibits Cdk2, Cdk3, Cdk4, and Cdk6 kinases (Ki 0.5-15 nM) but is much less effective toward Cdc2/cyclin B (Ki approximately 400 nM) and Cdk5/p35 (Ki > 2 microM), and does not associate with Cdk7/cyclin H. Overexpression of P21 arrests cells in G1. Thus, p21 is not a universal inhibitor of Cdks but displays selectivity for G1/S Cdk/cyclin complexes. Association of p21 with Cdks is greatly enhanced by cyclin binding. This property is shared by the structurally related inhibitor p27, suggesting a common biochemical mechanism for inhibition. With respect to Cdk2 and Cdk4 complexes, p27 shares the inhibitory potency of p21 but has slightly different kinase specificities. In normal diploid fibroblasts, the vast majority of active Cdk2 is associated with p21, but this active kinase can be fully inhibited by addition of exogenous p21. Reconstruction experiments using purified components indicate that multiple molecules of p21 can associate with Cdk/cyclin complexes and inactive complexes contain more than one molecule of p21. Together, these data suggest a model whereby p21 functions as an inhibitory buffer whose levels determine the threshold kinase activity required for cell cycle progression.

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Egan, Elizabeth A., and Mark J. Solomon. "Cyclin-Stimulated Binding of Cks Proteins to Cyclin-Dependent Kinases." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 3659–67. http://dx.doi.org/10.1128/mcb.18.7.3659.

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ABSTRACT Although Cks proteins were the first identified binding partners of cyclin-dependent protein kinases (cdks), their cell cycle functions have remained unclear. To help elucidate the function of Cks proteins, we examined whether their binding to p34 cdc2 (the mitotic cdk) varies during the cell cycle in Xenopusegg extracts. We observed that binding of human CksHs2 to p34 cdc2 was stimulated by cyclin B. This stimulation was dependent on the activating phosphorylation of p34 cdc2 on Thr-161, which follows cyclin binding and is mediated by the cdk-activating kinase. Neither the inhibitory phosphorylations of p34 cdc2 nor the catalytic activity of p34 cdc2 was required for this stimulation. Stimulated binding of CksHs2 to another cdk, p33 cdk2 , required both cyclin A and activating phosphorylation. Our findings support recent models that suggest that Cks proteins target active forms of p34 cdc2 to substrates.

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17

Verde, F., M. Dogterom, E. Stelzer, E. Karsenti, and S. Leibler. "Control of microtubule dynamics and length by cyclin A- and cyclin B-dependent kinases in Xenopus egg extracts." Journal of Cell Biology 118, no. 5 (September 1, 1992): 1097–108. http://dx.doi.org/10.1083/jcb.118.5.1097.

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In eukaryotic cells, the onset of mitosis involves cyclin molecules which interact with proteins of the cdc2 family to produce active kinases. In vertebrate cells, cyclin A dependent kinases become active in S- and pro-phases, whereas a cyclin B-dependent kinase is mostly active in metaphase. It has recently been shown that, when added to Xenopus egg extracts, bacterially produced A- and B-type cyclins associate predominantly with the same kinase catalytic subunit, namely p34cdc2, and induce its histone H1 kinase activity with different kinetics. Here, we show that in the same cell free system, both the addition of cyclin A and cyclin B changes microtubule behavior. However, the cyclin A-dependent kinase does not induce a dramatic shortening of centrosome-nucleated microtubules whereas the cyclin B-dependent kinase does, as previously reported. Analysis of the parameters of microtubule dynamics by fluorescence video microscopy shows that the dramatic shortening induced by the cyclin B-dependent kinase is correlated with a several fold increase in catastrophe frequency, an effect not observed with the cyclin A-dependent kinase. Using a simple mathematical model, we show how the length distributions of centrosome-nucleated microtubules relate to the four parameters that describe microtubule dynamics. These four parameters define a threshold between unlimited microtubule growth and the establishment of steady-state dynamics, which implies that well defined steady-state length distributions can be produced by regulating precisely the respective values of the dynamical parameters. Moreover, the dynamical model predicts that increasing catastrophe frequency is more efficient than decreasing the rescue frequency to reduce the average steady state length of microtubules. These theoretical results are quantitatively confirmed by the experimental data.

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18

Zhang, H., Y. Xiong, and D. Beach. "Proliferating cell nuclear antigen and p21 are components of multiple cell cycle kinase complexes." Molecular Biology of the Cell 4, no. 9 (September 1993): 897–906. http://dx.doi.org/10.1091/mbc.4.9.897.

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We have recently shown that two proteins, proliferating cell nuclear antigen (PCNA) and p21, are associated with cyclin D. Here we show that PCNA and p21 are common components of a wide variety of cyclin/cyclin-dependent kinase complexes in nontransformed cells. These include kinase complexes containing cyclin A, cyclin B, and cyclin D, associated either with CDC2, CDK2, CDK4, or CDK5. We show that PCNA and p21 form separate quaternary complex with each cyclin/CDK and that these quaternary complexes contain a substantial, if not major, fraction of the cell cycle kinases in asynchronously growing cells. These results suggest that PCNA and p21 may perform a common function for all these kinases.

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19

Desai, D., Y. Gu, and D. O. Morgan. "Activation of human cyclin-dependent kinases in vitro." Molecular Biology of the Cell 3, no. 5 (May 1992): 571–82. http://dx.doi.org/10.1091/mbc.3.5.571.

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We have analyzed the activation of human cyclin-dependent kinases in a cell-free system. Human CDC2, cyclin-dependent kinase 2 (CDK2), cyclin A, and cyclin B1 were produced in insect cells by infection with recombinant baculoviruses. CDC2 or CDK2 monomers in lysates of infected cells could be activated by the addition of lysates containing cyclin A or B1. CDC2 activation by cyclin B1, as well as CDK2 activation by cyclins A and B1, was accompanied by the formation of high molecular weight complexes. In contrast, CDC2 did not bind effectively to cyclin A. CDC2 activation by cyclin B1 was studied in detail and was found to be accompanied by phosphorylation of CDC2 on Threonine 161. The binding of CDC2 to cyclin B1 also occurred under conditions where CDC2 phosphorylation was prevented, resulting in an inactive complex that could then be phosphorylated and activated on addition of cell extract. Highly purified CDC2 and cyclin B1 also formed inactive complexes that could be activated in an ATP-dependent fashion by unidentified components in crude cell extracts. These data suggest that the CDC2 activation process begins with cyclin binding, after which CDC2 phosphorylation, catalyzed by a separate enzyme, leads to activation.

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20

Fiano, Valentina, Chiara Ghimenti, and Davide Schiffer. "Expression of cyclins, cyclin-dependent kinases and cyclin-dependent kinase inhibitors in oligodendrogliomas in humans." Neuroscience Letters 347, no. 2 (August 2003): 111–15. http://dx.doi.org/10.1016/s0304-3940(03)00615-3.

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21

Lukas, J., J. Bartkova, and J. Bartek. "Convergence of mitogenic signalling cascades from diverse classes of receptors at the cyclin D-cyclin-dependent kinase-pRb-controlled G1 checkpoint." Molecular and Cellular Biology 16, no. 12 (December 1996): 6917–25. http://dx.doi.org/10.1128/mcb.16.12.6917.

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The commitment of mammalian cells in late G1 to replicate the genome and divide in response to mitogenic growth factors operating via tyrosine kinase receptors depends on phosphorylation of the retinoblastoma protein (pRb), a process controlled by cyclin D-associated cyclin-dependent kinases (cdks) and their inhibitors. This study addressed the issue of whether also other mitogenic signalling cascades require activation of cyclin D-associated kinases or whether any mitogenic pathway can bypass the cyclin D-pRb checkpoint. We show that mitogenic signal transduction pathways from three classes of receptors, the membrane tyrosine kinase receptors activated by serum mitogens or epidermal growth factor, estrogen receptors triggered by estradiol, and the cyclic AMP-dependent signalling from G-protein-coupled thyrotropin receptors, all converge and strictly require the cyclin D-cdk activity to induce S phase in human MCF-7 cells and/or primary dog thyrocytes. Combined microinjection and biochemical approaches showed that whereas these three mitogenic cascades are sensitive to the p16 inhibitor of cdk4/6 and/or cyclin D1-neutralizing antibody and able to induce pRb kinase activity, their upstream biochemical routes are distinct as demonstrated by their differential sensitivity to lovastatin and requirements for mitogen-activated protein kinases whose sustained activation is seen only in the growth factor-dependent pathway. Taken together, these results support the candidacy of the cyclin D-cdk-pRb interplay for the convergence step of multiple signalling cascades and a mechanism contributing to the restriction point switch.

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22

Choi, Y. J., and L. Anders. "Signaling through cyclin D-dependent kinases." Oncogene 33, no. 15 (May 6, 2013): 1890–903. http://dx.doi.org/10.1038/onc.2013.137.

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23

Malumbres, Marcos, Edward Harlow, Tim Hunt, Tony Hunter, Jill M. Lahti, Gerard Manning, David O. Morgan, Li-Huei Tsai, and Debra J. Wolgemuth. "Cyclin-dependent kinases: a family portrait." Nature Cell Biology 11, no. 11 (November 2009): 1275–76. http://dx.doi.org/10.1038/ncb1109-1275.

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24

Noble, Martin E. M., and Jane A. Endicott. "Chemical Inhibitors of Cyclin-Dependent Kinases." Pharmacology & Therapeutics 82, no. 2-3 (May 1999): 269–78. http://dx.doi.org/10.1016/s0163-7258(98)00051-5.

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25

Nigg, Erich A. "Targets of cyclin-dependent protein kinases." Current Opinion in Cell Biology 5, no. 2 (April 1993): 187–93. http://dx.doi.org/10.1016/0955-0674(93)90101-u.

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26

Meijer, Laurent. "Chemical inhibitors of cyclin-dependent kinases." Trends in Cell Biology 6, no. 10 (October 1996): 393–97. http://dx.doi.org/10.1016/0962-8924(96)10034-9.

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27

Knockaert, Marie, Paul Greengard, and Laurent Meijer. "Pharmacological inhibitors of cyclin-dependent kinases." Trends in Pharmacological Sciences 23, no. 9 (September 2002): 417–25. http://dx.doi.org/10.1016/s0165-6147(02)02071-0.

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28

Hardcastle, Ian R., Bernard T. Golding, and Roger J. Griffin. "DESIGNING INHIBITORS OF CYCLIN-DEPENDENT KINASES." Annual Review of Pharmacology and Toxicology 42, no. 1 (April 2002): 325–48. http://dx.doi.org/10.1146/annurev.pharmtox.42.090601.125940.

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29

LIU, F. "Smad3 phosphorylation by cyclin-dependent kinases." Cytokine & Growth Factor Reviews 17, no. 1-2 (February 2006): 9–17. http://dx.doi.org/10.1016/j.cytogfr.2005.09.010.

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30

Doonan, John H., and Georgios Kitsios. "Functional Evolution of Cyclin-Dependent Kinases." Molecular Biotechnology 42, no. 1 (January 15, 2009): 14–29. http://dx.doi.org/10.1007/s12033-008-9126-8.

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31

Gao, Chun Y., and Peggy S. Zelenka. "Cyclins, cyclin-dependent kinases and differentiation." BioEssays 19, no. 4 (April 1997): 307–15. http://dx.doi.org/10.1002/bies.950190408.

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32

Tian, Jean Q., and Andrea Quaroni. "Involvement of p21(WAF1/Cip1) and p27(Kip1) in intestinal epithelial cell differentiation." American Journal of Physiology-Cell Physiology 276, no. 6 (June 1, 1999): C1245—C1258. http://dx.doi.org/10.1152/ajpcell.1999.276.6.c1245.

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Using the conditionally immortalized human cell line tsFHI, we have investigated the role of cyclin-dependent kinase inhibitors (CKIs) in intestinal epithelial cell differentiation. Expression of cyclins, cyclin-dependent kinases (Cdk), and CKIs was examined under conditions promoting growth, growth arrest, or expression of differentiated traits. Formation of complexes among cell cycle regulatory proteins and their kinase activities were also investigated. The tsFHI cells express three CKIs: p16, p21, and p27. With differentiation, p21 and p27 were strongly induced, but with different kinetics: the p21 increase was rapid but transient and the p27 increase was delayed but sustained. Our results suggest that the function of p16 is primarily to inhibit cyclin D-associated kinases, making tsFHI cells dependent on cyclin E-Cdk2 for pRb phosphorylation and G1/S progression. Furthermore, they indicate that p21 is the main CKI involved in irreversible growth arrest during the early stages of cell differentiation in association with D-type cyclins, cyclin E, and Cdk2, whereas p27 may induce or stabilize expression of differentiated traits acting independently of cyclin-Cdk function.

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Tsakraklides, Vasiliki, and Mark J. Solomon. "Comparison of Cak1p-like Cyclin-dependent Kinase-activating Kinases." Journal of Biological Chemistry 277, no. 36 (June 25, 2002): 33482–89. http://dx.doi.org/10.1074/jbc.m205537200.

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Preisinger, Christian, and Francis A. Barr. "Kinases regulating Golgi apparatus structure and function." Biochemical Society Symposia 72 (January 1, 2005): 15–30. http://dx.doi.org/10.1042/bss0720015.

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Protein kinases control Golgi function in both mitotic and interphase cells. In mitosis, phosphorylation of structural proteins by Cdk1 (cyclin-dependent kinase 1)-cyclin B, Polo-like and mitogen-activated protein kinases underlie changes in Golgi reorganization during cell division. While in interphase, signalling pathways that are associated with the Golgi control secretory function through a variety of mechanisms. Some of these, notably those involving protein kinase D and Ste20 family kinases, are also relevant for the establishment and maintenance of cell polarization and migration.

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Woo, M. S., I. Sánchez, and B. D. Dynlacht. "p130 and p107 use a conserved domain to inhibit cellular cyclin-dependent kinase activity." Molecular and Cellular Biology 17, no. 7 (July 1997): 3566–79. http://dx.doi.org/10.1128/mcb.17.7.3566.

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The pRB-related proteins p107 and p130 are thought to suppress growth in part through their associations with two important cell cycle kinases, cyclin A-cdk2 and cyclin E-cdk2, and transcription factor E2F. Although each protein plays a critical role in cell proliferation, the functional consequences of the association among growth suppressor, cyclin-dependent kinase, and transcription factor have remained elusive. In an attempt to understand the biochemical properties of such complexes, we reconstituted each of the p130-cyclin-cdk2 and p107-cyclin-cdk2 complexes found in vivo with purified, recombinant proteins. Strikingly, stoichiometric association of p107 or p130 with either cyclin E-cdk2 or cyclin A-cdk2 negated the activities of these kinases. The results of our experiments suggest that inhibition does not result from substrate competition or loss of cdk2 activation. Kinase inhibitory activity was dependent upon an amino-terminal region of p107 that is highly conserved with p130. Further, a role for this amino-terminal region in growth suppression was uncovered by using p107 mutants unable to bind E2F. To determine whether cellular complexes might display similar regulatory properties, we purified p130-cyclin A-cdk2 complexes from human cells and found that such complexes exist in two forms, one that contains E2F-4-DP-1 and one that lacks the heterodimer. These endogenous complexes behaved like the in vitro-reconstituted complexes, exhibiting low levels of associated kinase activity that could be significantly augmented by dissociation of p130. The results of these experiments suggest a mechanism whereby p130 and p107 suppress growth by inhibiting important cell cycle kinases.

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36

Jeannon, J. P., and J. A. Wilson. "Cyclins, cyclin-dependent kinases, cyclin-dependent kinase inhibitors and their role in head and neck cancer." Clinical Otolaryngology and Allied Sciences 23, no. 5 (October 1998): 420–24. http://dx.doi.org/10.1046/j.1365-2273.1998.00182.x.

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37

Huang, H.-H., C.-H. Chen, S.-C. Huang, C.-H. Yang, and C.-F. Hwang. "Expression of 14-3-3 sigma, cyclin-dependent kinases 2 and 4, p16, and Epstein–Barr nuclear antigen 1 in nasopharyngeal carcinoma." Journal of Laryngology & Otology 128, no. 2 (January 24, 2014): 134–41. http://dx.doi.org/10.1017/s0022215113003447.

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AbstractObjective:The protein 14-3-3 sigma plays a role in cell cycle arrest by sequestering cyclin-dependent kinase 1 cyclin B1 complexes, as well as cyclin-dependent kinases 2 and 4, hence its definition as a cyclin-dependent kinase inhibitor. However, the nature of the interaction between these biological markers in nasopharyngeal carcinoma is unknown. This study aimed to investigate whether altered expression of these markers contributes to nasopharyngeal carcinogenesis.Methods:The study population consisted of 30 nasopharyngeal carcinoma patients and 10 patients without nasopharyngeal carcinoma. The nasopharyngeal carcinoma cell lines TW02, TW04 and Hone-1 were also assessed. We analysed levels of messenger RNA and protein for the p16 gene and the 14-3-3 sigma, Epstein–Barr nuclear antigen 1, and cyclin-dependent kinase 2 and 4 proteins, in nasopharyngeal carcinoma tissue specimens and cell lines and in normal nasopharyngeal tissue.Results:Protein and messenger RNA levels for cyclin-dependent kinase 2 and Epstein–Barr nuclear antigen 1 were significantly higher in nasopharyngeal carcinoma compared with normal tissue, while levels of cyclin-dependent kinase 4 generally were not; results for 14-3-3 sigma varied. Nasopharyngeal carcinoma patients had diminished p16 gene expression, compared with normal tissue.Conclusion:Levels of cyclin-dependent kinase 2 and Epstein–Barr nuclear antigen 1 were significantly higher in nasopharyngeal carcinoma than in normal tissue, while p16 gene expression was diminished. These three proteins may contribute to nasopharyngeal carcinogenesis.

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38

Sweeney, C., M. Murphy, M. Kubelka, S. E. Ravnik, C. F. Hawkins, D. J. Wolgemuth, and M. Carrington. "A distinct cyclin A is expressed in germ cells in the mouse." Development 122, no. 1 (January 1, 1996): 53–64. http://dx.doi.org/10.1242/dev.122.1.53.

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In this paper, the existence of two A-type cyclins in the mouse is demonstrated. In the adult mouse, the expression of cyclin A1, which has greatest sequence identity with Xenopus cyclin A1, is restricted to germ cells. In contrast cyclin A2, which has greatest sequence identity with human cyclin A and Xenopus cyclin A2, is expressed in all tissues analysed. In order to explore the function of cyclin A1 in germ cells, its expression during the meiotic cell cycle and its associated kinase subunits have been characterised in the testis. The levels of cyclin A1 mRNA rise dramatically in late pachytene spermatocytes and become undetectable soon after completion of the meiotic divisions; thus its expression is cell cycle regulated. In lysates of germ cells from adult testes, cyclin A1 is present in p13suc1 precipitates, and cyclin A1 immunoprecipitates possess histone H1 kinase activity. Three kinase partners of cyclin A1 were identified: p34cdc2, a polypeptide of 39 × 10(3) M(r) that is related to p33cdk2 and, in lesser quantities, p33cdk2. Cyclin A1 was also detected in oocytes; in metaphase I and metaphase II oocytes, a proportion of the cyclin A1 colocalises with the spindle, possibly suggestive of a functional interaction. These data indicate that mammalian germ cells contain cyclin A1-dependent kinases that either act as a substitute for, or in addition to, the cyclin A2-dependent kinases characterised in somatic tissues.

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Wang, Shixiong, Sachin Singh, Madhumohan Katika, Sandra Lopez-Aviles, and Antoni Hurtado. "High Throughput Chemical Screening Reveals Multiple Regulatory Proteins on FOXA1 in Breast Cancer Cell Lines." International Journal of Molecular Sciences 19, no. 12 (December 19, 2018): 4123. http://dx.doi.org/10.3390/ijms19124123.

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Forkhead box A1 (FOXA1) belongs to the forkhead class transcription factor family, playing pioneering function for hormone receptors in breast and prostate cancers, and mediating activation of linage specific enhancers. Interplay between FOXA1 and breast cancer specific signaling pathways has been reported previously, indicating a regulation network on FOXA1 in breast cancer cells. Here in this study, we aimed to identify which are the proteins that could potentially control FOXA1 function in breast cancer cell lines expressing different molecular markers. We first established a luciferase reporter system reflecting FOXA1 binding to DNA. Then, we applied high throughput chemical screening of multiple protein targets and mass spectrometry in breast cancer cell lines expressing different molecular markers: ER positive/HER2 negative (MCF-7), ER positive/HER2 positive (BT474), and ER negative/HER2 positive (MDA-MB-453). Regardless of estrogen receptor status, HER2 (human epidermal growth factor receptor 2) enriched cell lines showed similar response to kinase inhibitors, indicating the control of FOXA1 by cell signaling kinases. Among these kinases, we identified additional receptor tyrosine kinases and cyclin-dependent kinases as regulators of FOXA1. Furthermore, we performed proteomics experiments from FOXA1 inmunoprecipitated protein complex to identify that FOXA1 interacts with several proteins. Among all the targets, we identified cyclin-dependent kinase 1 (CDK1) as a positive factor to interact with FOXA1 in BT474 cell line. In silico analyses confirmed that cyclin-dependent kinases might be the kinases responsible for FOXA1 phosphorylation at the Forkhead domain and the transactivation domain. These results reveal that FOXA1 is potentially regulated by multiple kinases. The cell cycle control kinase CDK1 might control directly FOXA1 by phosphorylation and other kinases indirectly by means of regulating other proteins.

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Hirai, H., and C. J. Sherr. "Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1." Molecular and Cellular Biology 16, no. 11 (November 1996): 6457–67. http://dx.doi.org/10.1128/mcb.16.11.6457.

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The cyclin D-dependent kinases CDK4 and CDK6 trigger phosphorylation of the retinoblastoma protein (RB) late in G1 phase, helping to cancel its growth-suppressive function and thereby facilitating S-phase entry. Although specific inhibition of cyclin D-dependent kinase activity in vivo can prevent cells from entering S phase, it does not affect S-phase entry in cells lacking functional RB, implying that RB may be the only substrate of CDK4 and CDK6 whose phosphorylation is necessary for G1 exit. Using a yeast two-hybrid interactive screen, we have now isolated a novel cyclin D-interacting myb-like protein (designated DMP1), which binds specifically to the nonamer DNA consensus sequences CCCG(G/T)ATGT to activate transcription. A subset of these DMP1 recognition sequences containing a GGA trinucleotide core can also function as Ets-responsive elements. DMP1 mRNA and protein are ubiquitously expressed throughout the cell cycle in mouse tissues and in representative cell lines. DMP1 binds to D-type cyclins directly in vitro and when coexpressed in insect Sf9 cells. In both settings, it can be phosphorylated by cyclin D-dependent kinases, suggesting that its transcriptional activity may normally be regulated through such mechanisms. These results raise the possibility that cyclin D-dependent kinases regulate gene expression in an RB independent manner, thereby serving to link other genetic programs to the cell cycle clock.

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Albrecht, Jeffrey H., Brenda M. Rieland, Christopher J. Nelsen, and Cory L. Ahonen. "Regulation of G1 cyclin-dependent kinases in the liver: role of nuclear localization and p27 sequestration." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 6 (December 1, 1999): G1207—G1216. http://dx.doi.org/10.1152/ajpgi.1999.277.6.g1207.

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Recent studies suggest that cyclin D1 mediates progression of hepatocytes through G1 phase of the cell cycle. The present study further examines the regulation of cyclin D1-dependent kinase activity and the interplay between cyclin D1 and other G1phase regulatory proteins during liver regeneration. After 70% partial hepatectomy in rats, there was upregulation of kinase activity associated with cyclins (A, D1, D3, and E), cyclin-dependent kinases (Cdk2 and Cdk4), and Cdk-inhibitory proteins (p27, p107, and p130). Although cyclin D1/Cdk4 complexes were more abundant in the cytoplasmic fraction after partial hepatectomy, kinase activity was detected primarily in the nuclear fraction. Cytoplasmic cyclin D1/Cdk4 complexes were activated by recombinant cyclin H/Cdk7. Because endogenous Cdk7 activity was found in the nucleus, this suggests that activation of cyclin D1/Cdk4 requires nuclear importation and subsequent phosphorylation by cyclin H/Cdk7. Recombinant cyclin E/Cdk2 was inhibited by extracts from quiescent liver, and cyclin D1 could titrate out this inhibitory activity. Induction of cyclin D1 was accompanied by increased abundance of cyclin D1/p27 complexes, and most p27 was sequestered by cyclin D1 after partial hepatectomy. Thus cyclin D1 appears to play two roles during G1 phase progression in the regenerating liver: it forms a nuclear kinase complex, and it promotes activation of Cdk2 by sequestering inhibitory proteins such as p27. These experiments underscore the complexity of cyclin/Cdk regulatory networks in the regenerating liver.

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Kciuk, Mateusz, Adrianna Gielecińska, Somdutt Mujwar, Mariusz Mojzych, and Renata Kontek. "Cyclin-dependent kinases in DNA damage response." Biochimica et Biophysica Acta (BBA) - Reviews on Cancer 1877, no. 3 (May 2022): 188716. http://dx.doi.org/10.1016/j.bbcan.2022.188716.

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Morgan, David O. "CYCLIN-DEPENDENT KINASES: Engines, Clocks, and Microprocessors." Annual Review of Cell and Developmental Biology 13, no. 1 (November 1997): 261–91. http://dx.doi.org/10.1146/annurev.cellbio.13.1.261.

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Naula, C., R. J. Ford, and J. C. Mottram. "Analysis of Trypanosoma brucei cyclin-dependent kinases." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A482. http://dx.doi.org/10.1042/bst028a482c.

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Zhou, Qi. "Targeting Cyclin-Dependent Kinases in Ovarian Cancer." Cancer Investigation 35, no. 6 (April 13, 2017): 367–76. http://dx.doi.org/10.1080/07357907.2017.1283508.

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Galbraith, Matthew D., Heather Bender, and Joaquín M. Espinosa. "Therapeutic targeting of transcriptional cyclin-dependent kinases." Transcription 10, no. 2 (November 9, 2018): 118–36. http://dx.doi.org/10.1080/21541264.2018.1539615.

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Sherr, C. J., and J. M. Roberts. "Inhibitors of mammalian G1 cyclin-dependent kinases." Genes & Development 9, no. 10 (May 15, 1995): 1149–63. http://dx.doi.org/10.1101/gad.9.10.1149.

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Endicott, Jane A., Martin EM Noble, and Julie A. Tucker. "Cyclin-dependent kinases: inhibition and substrate recognition." Current Opinion in Structural Biology 9, no. 6 (December 1999): 738–44. http://dx.doi.org/10.1016/s0959-440x(99)00038-x.

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Errico, Alessia, Krupa Deshmukh, Yoshimi Tanaka, Andrei Pozniakovsky, and Tim Hunt. "Identification of substrates for cyclin dependent kinases." Advances in Enzyme Regulation 50, no. 1 (2010): 375–99. http://dx.doi.org/10.1016/j.advenzreg.2009.12.001.

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Jorda, Radek, Eva Schütznerová, Petr Cankař, Veronika Brychtová, Jana Navrátilová, and Vladimír Kryštof. "Novel arylazopyrazole inhibitors of cyclin-dependent kinases." Bioorganic & Medicinal Chemistry 23, no. 9 (May 2015): 1975–81. http://dx.doi.org/10.1016/j.bmc.2015.03.025.

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Journal articles on the topic 'Cyclin-dependent kinases'

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