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Relevant bibliographies by topics / NIMA-like kinase

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Academic literature on the topic 'NIMA-like kinase'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "NIMA-like kinase"

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Swenson, Katherine I., Katharine E. Winkler, and Anthony R. Means. "A New Identity for MLK3 as an NIMA-related, Cell Cycle–regulated Kinase That Is Localized near Centrosomes and Influences Microtubule Organization." Molecular Biology of the Cell 14, no. 1 (2003): 156–72. http://dx.doi.org/10.1091/mbc.e02-02-0115.

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Although conserved counterparts for most proteins involved in the G2/M transition of the cell cycle have been found in all eukaryotes, a notable exception is the essential but functionally enigmatic fungal kinase NIMA. While a number of vertebrate kinases have been identified with catalytic domain homology to NIMA, none of these resemble NIMA within its extensive noncatalytic region, a region critical for NIMA function in Aspergillus nidulans. We used a bioinformatics approach to search for proteins with homology to the noncatalytic region of NIMA and identified mixed lineage kinase 3 (MLK3).

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Davies, Jonathan R., Aysha H. Osmani, Colin P. C. De Souza, Catherine Bachewich, and Stephen A. Osmani. "Potential Link between the NIMA Mitotic Kinase and Nuclear Membrane Fission during Mitotic Exit in Aspergillus nidulans." Eukaryotic Cell 3, no. 6 (2004): 1433–44. http://dx.doi.org/10.1128/ec.3.6.1433-1444.2004.

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ABSTRACT We have isolated TINC as a NIMA-interacting protein by using the yeast two-hybrid system and have confirmed that TINC interacts with NIMA in Aspergillus nidulans. The TINC-NIMA interaction is stabilized in the absence of phosphatase inhibitors and in the presence of kinase-inactive NIMA, suggesting that the interaction is enhanced when NIMA is not fully activated. TINC is a cytoplasmic protein. TINC homologues and a TINC-like protein (A. nidulans HETC) are conserved in other filamentous fungi. Neither deletion of tinC nor deletion of both tinC and A. nidulans hetC is lethal, but delet

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Krien, M. J., S. J. Bugg, M. Palatsides, G. Asouline, M. Morimyo, and M. J. O'Connell. "A NIMA homologue promotes chromatin condensation in fission yeast." Journal of Cell Science 111, no. 7 (1998): 967–76. http://dx.doi.org/10.1242/jcs.111.7.967.

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Entry into mitosis requires p34(cdc2), which activates downstream mitotic events through phosphorylation of key target proteins. In Aspergillus nidulans, the NIMA protein kinase has been identified as a potential downstream target and plays a role in regulating chromatin condensation at mitosis. nimA- mutants arrest in a state that physically resembles interphase even though p34(cdc2) is fully active. Despite evidence for the existence of NIMA-like activities in a variety of cell types, the only bona fide NIMA homologue that has been identified is the nim-1 gene of Neurospora crassa. We report

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Lies, C. M., J. Cheng, S. W. James, N. R. Morris, M. J. O'Connell, and P. M. Mirabito. "BIMAAPC3, a component of the Aspergillus anaphase promoting complex/cyclosome, is required for a G2 checkpoint blocking entry into mitosis in the absence of NIMA function." Journal of Cell Science 111, no. 10 (1998): 1453–65. http://dx.doi.org/10.1242/jcs.111.10.1453.

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Temperature sensitive (ts) nimA mutants of Aspergillus nidulans arrest at a unique point in G2 which is post activation of CDC2. Here we show that this G2 arrest is due to loss of nimA function and that it is dependent on BIMAAPC3, a component of the anaphase promoting complex/cyclosome (APC/C). Whereas nimA single mutants arrested in G2 with decondensed chromatin and interphase microtubule arrays, nimA, bimAAPC3 double mutants arrested growth with condensed chromatin and aster-like microtubule arrays. nimA, bimAAPC3 double mutants entered mitosis with kinetics similar to bimAAPC3 single mutan

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Shen, Kuo-Fang, and Stephen A. Osmani. "Regulation of mitosis by the NIMA kinase involves TINA and its newly discovered partner, An-WDR8, at spindle pole bodies." Molecular Biology of the Cell 24, no. 24 (2013): 3842–56. http://dx.doi.org/10.1091/mbc.e13-07-0422.

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The NIMA kinase is required for mitotic nuclear pore complex disassembly and potentially controls other mitotic-specific events. To investigate this possibility, we imaged NIMA–green fluorescent protein (GFP) using four-dimensional spinning disk confocal microscopy. At mitosis NIMA-GFP locates to spindle pole bodies (SPBs), which contain Cdk1/cyclin B, followed by Aurora, TINA, and the BimC kinesin. NIMA promotes NPC disassembly in a spatially regulated manner starting near SPBs. NIMA is also required for TINA, a NIMA-interacting protein, to locate to SPBs during initiation of mitosis, and TIN

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6

Ukil, Leena, Archana Varadaraj, Meera Govindaraghavan, Hui-Lin Liu, and Stephen A. Osmani. "Copy Number Suppressors of the Aspergillus nidulans nimA1 Mitotic Kinase Display Distinctive and Highly Dynamic Cell Cycle-Regulated Locations." Eukaryotic Cell 7, no. 12 (2008): 2087–99. http://dx.doi.org/10.1128/ec.00278-08.

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ABSTRACT The Aspergillus nidulans NIMA kinase is essential for mitosis and is the founding member of the conserved NIMA-related kinase (Nek) family of protein kinases. To gain insight into NIMA function, a copy number suppression screen has been completed that defines three proteins termed MCNA, MCNB, and MCNC (multi-copy-number suppressor of nimA1 A, B, and C). All display a distinctive and dynamic cell cycle-specific distribution. MCNC has weak similarity to Saccharomyces cerevisiae Def1 within a shared CUE-like domain. MCNC, like Def1, is a cytoplasmic protein with slow mobility during sodi

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Xia, Jiliang, Reinaldo Franqui Machin, Zhimin Gu, and Fenghuang Zhan. "Role of NEK2A in Human Cancer and Its Therapeutic Potentials." BioMed Research International 2015 (2015): 1–12. http://dx.doi.org/10.1155/2015/862461.

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Chromosome instability (CIN) has been identified as a common feature of most human cancers. A number of centrosomal kinases are thought to cause CIN in cancer cells. Part of those centrosomal kinases exhibit elevated expression in a wide variety of tumours and cancer cell lines. Additionally, critical roles in many aspects of cancer cell growth, proliferation, metastasis, and drug resistance have been assigned to some of these centrosomal kinases, such as polo-like kinase 1 (PLk1) and Aurora-A kinase. Recent studies from our group and others revealed that a centrosomal kinase, Never in Mitosis

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Dodson, Charlotte A., Tamanna Haq, Sharon Yeoh, Andrew M. Fry, and Richard Bayliss. "The structural mechanisms that underpin mitotic kinase activation." Biochemical Society Transactions 41, no. 4 (2013): 1037–41. http://dx.doi.org/10.1042/bst20130066.

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In eukaryotic cells, the peak of protein phosphorylation occurs during mitosis, switching the activities of a significant proportion of proteins and orchestrating a wholesale reorganization of cell shape and internal architecture. Most mitotic protein phosphorylation events are catalysed by a small subset of serine/threonine protein kinases. These include members of the Cdk (cyclin-dependent kinase), Plk (Polo-like kinase), Aurora, Nek (NimA-related kinase) and Bub families, as well as Haspin, Greatwall and Mps1/TTK. There has been steady progress in resolving the structural mechanisms that re

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ZHANG, H., G. SCOFIELD, P. FOBERT, and J. H. DOONAN. "A nimA‐like protein kinase transcript is highly expressed in meristems of Antirrhinum majus." Journal of Microscopy 181, no. 2 (1996): 186–94. http://dx.doi.org/10.1046/j.1365-2818.1996.110390.x.

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Ma, Hoi Tang, and Randy Y. C. Poon. "How protein kinases co-ordinate mitosis in animal cells." Biochemical Journal 435, no. 1 (2011): 17–31. http://dx.doi.org/10.1042/bj20100284.

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Mitosis is associated with profound changes in cell physiology and a spectacular surge in protein phosphorylation. To accomplish these, a remarkably large portion of the kinome is involved in the process. In the present review, we will focus on classic mitotic kinases, such as cyclin-dependent kinases, Polo-like kinases and Aurora kinases, as well as more recently characterized players such as NIMA (never in mitosis in Aspergillus nidulans)-related kinases, Greatwall and Haspin. Together, these kinases co-ordinate the proper timing and fidelity of processes including centrosomal functions, spi

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Dissertations / Theses on the topic "NIMA-like kinase"

1

Schütz, Martin Maximilian. "The role of NIMA-like kinase Nek9 in mitosis." Doctoral thesis, Universitat Pompeu Fabra, 2011. http://hdl.handle.net/10803/38705.

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Mitosis is the essential process during which a cell divides into two viable daughter cells. To allow a faithful segregation of the chromosomes into each daughter, the cell forms the bipolar spindle. The NIMA-like kinase family member Nek9 has been previously proposed to play a role in bipolar spindle assembly and in the chromosomal pathway of microtubule assembly. We aimed at gaining a better understanding of Nek9 function by characterizing Xenopus Nek9, xNek9, using the Xenopus egg extract system. We have shown that xNek9 may not act through the kinase cascade xNek9 – xNek6 in meiosis as

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Agueci, Francesco [Verfasser], Klaus [Akademischer Betreuer] Pillen, Andreas [Akademischer Betreuer] Houben, and Helmut [Akademischer Betreuer] Bäumlein. "Characterization of NIMA-like kinases in Arabidopsis thaliana / Francesco Agueci. Betreuer: Klaus Pillen ; Andreas Houben ; Helmut Bäumlein." Halle, Saale : Universitäts- und Landesbibliothek Sachsen-Anhalt, 2010. http://d-nb.info/1025010876/34.

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