Relevant bibliographies by topics / Calcineurine B-like

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Academic literature on the topic 'Calcineurine B-like'

Author: Grafiati
Published: 4 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "Calcineurine B-like"

1

Luan, Sheng, Jörg Kudla, Manuel Rodriguez-Concepcion, Shaul Yalovsky, and Wilhelm Gruissem. "Calmodulins and Calcineurin B–like Proteins." Plant Cell 14, suppl 1 (May 2002): S389—S400. http://dx.doi.org/10.1105/tpc.001115.

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沈, 清. "Calcineurin B-Like Proteins and Their Interacting Protein Kinases." Botanical Research 01, no. 02 (2012): 9–12. http://dx.doi.org/10.12677/br.2012.12002.

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Cottle, Wayne Taylor, Clarice Hayley Wallert, Kristine Kay Anderson, Michelle Fang Tran, Clare Loraine Bakker, Mark Anthony Wallert, and Joseph John Provost. "Calcineurin homologous protein isoform 2 supports tumor survival via the sodium hydrogen exchanger isoform 1 in non-small cell lung cancer." Tumor Biology 42, no. 7 (July 2020): 101042832093786. http://dx.doi.org/10.1177/1010428320937863.

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Maintaining intracellular pH is crucial for preserving healthy cellular behavior and, when dysregulated, results in increased proliferation, migration, and invasion. The Na+/H+ exchanger isoform 1 is a highly regulated transmembrane antiporter that maintains pH homeostasis by exporting protons in response to intra- and extracellular signals. Activation of Na+/H+ exchanger isoform 1 is exquisitely regulated by the extracellular environment and protein cofactors, including calcineurin B homologous proteins 1 and 2. While Na+/H+ exchanger isoform 1 and calcineurin B homologous protein 1 are ubiquitously expressed, calcineurin B homologous protein 2 shows tissue-specific expression and upregulation in a variety of cancer cells. In addition, calcineurin B homologous protein 2 expression is modulated by tumorigenic extracellular conditions like low nutrients. To understand the role of calcineurin B homologous protein 2 in tumorigenesis and survival in lung cancer, we surveyed existing databases and formed a comprehensive report of Na+/H+ exchanger isoform 1, calcineurin B homologous protein 1, and calcineurin B homologous protein 2 expression in diseased and non-diseased tissues. We show that calcineurin B homologous protein 2 is upregulated during oncogenesis in many adeno and squamous carcinomas. To understand the functional role of calcineurin B homologous protein 2 upregulation, we evaluated the effect of Na+/H+ exchanger isoform 1 and calcineurin B homologous protein 2 depletion on cellular function during cancer progression in situ. Here, we show that calcineurin B homologous protein 2 functions through Na+/H+ exchanger isoform 1 to effect cell proliferation, cell migration, steady-state pH i, and anchorage-independent tumor growth. Finally, we present evidence that calcineurin B homologous protein 2 depletion in vivo has potential to reduce tumor burden in a xenograft model. Together, these data support the tumor-promoting potential of aberrant calcineurin B homologous protein 2 expression and position calcineurin B homologous protein 2 as a potential therapeutic target for the treatment of non-small cell lung cancer.
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Bucher, Philip, Tabea Erdmann, Paula Grondona, Wendan Xu, Anja Schmitt, Christoph Schürch, Myroslav Zapukhlyak, et al. "Targeting chronic NFAT activation with calcineurin inhibitors in diffuse large B-cell lymphoma." Blood 135, no. 2 (January 9, 2020): 121–32. http://dx.doi.org/10.1182/blood.2019001866.

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Abstract Diffuse large B-cell lymphoma (DLBCL) represents the most common adult lymphoma and can be divided into 2 major molecular subtypes: the germinal center B-cell-like and the aggressive activated B-cell-like (ABC) DLBCL. Previous studies suggested that chronic B-cell receptor signaling and increased NF-κB activation contribute to ABC DLBCL survival. Here we show that the activity of the transcription factor NFAT is chronically elevated in both DLBCL subtypes. Surprisingly, NFAT activation is independent of B-cell receptor signaling, but mediated by an increased calcium flux and calcineurin-mediated dephosphorylation of NFAT. Intriguingly, although NFAT is activated in both DLBCL subtypes, long-term calcineurin inhibition with cyclosporin A or FK506, both clinically approved drugs, triggers potent cytotoxicity specifically in ABC DLBCL cells. The antitumor effects of calcineurin inhibitors are associated with the reduced expression of c-Jun, interleukin-6, and interleukin-10, which were identified as NFAT target genes that are particularly important for the survival of ABC DLBCL. Furthermore, calcineurin blockade synergized with BCL-2 and MCL-1 inhibitors in killing ABC DLBCL cells. Collectively, these findings identify constitutive NFAT signaling as a crucial functional driver of ABC DLBCL and highlight calcineurin inhibition as a novel strategy for the treatment of this aggressive lymphoma subtype.
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Batistič, Oliver, and Jörg Kudla. "Plant calcineurin B-like proteins and their interacting protein kinases." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 6 (June 2009): 985–92. http://dx.doi.org/10.1016/j.bbamcr.2008.10.006.

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Liu, Hao, Yong-Xin Wang, Hui Li, Rui-Min Teng, Yu Wang, and Jing Zhuang. "Genome-Wide Identification and Expression Analysis of Calcineurin B-Like Protein and Calcineurin B-Like Protein-Interacting Protein Kinase Family Genes in Tea Plant." DNA and Cell Biology 38, no. 8 (August 2019): 824–39. http://dx.doi.org/10.1089/dna.2019.4697.

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Ho, Viet The, Anh Nguyet Tran, Francesco Cardarelli, Pierdomenico Perata, and Chiara Pucciariello. "A calcineurin B-like protein participates in low oxygen signalling in rice." Functional Plant Biology 44, no. 9 (2017): 917. http://dx.doi.org/10.1071/fp16376.

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Following the identification of the calcineurin B-like interacting protein kinase 15 (CIPK15), which is a regulator of starch degradation, the low O2 signal elicited during rice germination under submergence has been linked to the sugar sensing cascade and calcium (Ca2+) signalling. CIPK proteins are downstream effectors of calcineurin B-like proteins (CBLs), which act as Ca2+ sensors, whose role under low O2 has yet to be established. In the present study we describe CBL4 as a putative CIPK15 partner, transcriptionally activated under low O2 in rice coleoptiles. The transactivation of the rice embryo CBL4 transcript and CBL4 promoter was influenced by the Ca2+ blocker ruthenium red (RR). The bimolecular fluorescence complementation (BiFC) assay associated to fluorescence recovery after photobleaching (FRAP) analysis confirmed that CBL4 interacts with CIPK15. The CBL4-CIPK15 complex is localised in the cytoplasm and the plasma-membrane. Experiments in protoplasts showed a dampening of α-amylase 3 (RAMY3D) expression after CBL4 silencing by artificial miRNA. Our results suggest that under low O2, the Ca2+ sensor CBL4 interacts with CIPK15 to regulate RAMY3D expression in a Ca2+-dependent manner.
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Mukai, Hideyuki, Chang-Duk Chang, Hozumi Tanaka, Akira Ito, Takayoshi Kuno, and Chikako Tanaka. "cDNA cloning of a novel testis-specific calcineurin B-like protein." Biochemical and Biophysical Research Communications 179, no. 3 (September 1991): 1325–30. http://dx.doi.org/10.1016/0006-291x(91)91718-r.

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Cyert, M. S., and J. Thorner. "Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone." Molecular and Cellular Biology 12, no. 8 (August 1992): 3460–69. http://dx.doi.org/10.1128/mcb.12.8.3460.

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By using an assay specific for detection of calcineurin, a Ca2+/calmodulin-dependent phosphoprotein phosphatase, this enzyme was purified approximately 5,000-fold from extracts of the yeast Saccharomyces cerevisiae. Cna1p and Cna2p, the products of two yeast genes encoding the catalytic (A) subunits of calcineurin, were major constituents of the purified fraction. A third prominent component of apparent molecular mass 16 kDa displayed several properties, including ability to bind 45Ca2+, that are characteristic of the regulatory (B) subunit of mammalian calcineurin and was recognized by an antiserum raised against bovine calcineurin. These antibodies were used to isolate the structural gene (CNB1) encoding this protein from a yeast expression library in the vector lambda gt11. The nucleotide sequence of CNB1 predicted a polypeptide similar in length and highly related in amino acid sequence (56% identity) to the mammalian calcineurin B subunit. Like its counterpart in higher cells, yeast Cnb1p was myristoylated at its N terminus. Mutants lacking Cnb1p, or all three calcineurin subunits (Cna1p, Cna2p, and Cnb1p), were viable. Extracts of cnb1 delta mutants contained no detectable calcineurin activity, even though Cna1p and Cna2p were present at normal levels, suggesting that the B subunit is required for full enzymatic activity in vitro. As was observed previously for MATa cna1 cna2 double mutants, MATa cnb1 mutants were defective in their ability to recover from alpha-factor-induced growth arrest. Thus, the B subunit also is required for the function of calcineurin in promoting adaptation of haploid yeast cells to pheromone in vivo.
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Cyert, M. S., and J. Thorner. "Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone." Molecular and Cellular Biology 12, no. 8 (August 1992): 3460–69. http://dx.doi.org/10.1128/mcb.12.8.3460-3469.1992.

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By using an assay specific for detection of calcineurin, a Ca2+/calmodulin-dependent phosphoprotein phosphatase, this enzyme was purified approximately 5,000-fold from extracts of the yeast Saccharomyces cerevisiae. Cna1p and Cna2p, the products of two yeast genes encoding the catalytic (A) subunits of calcineurin, were major constituents of the purified fraction. A third prominent component of apparent molecular mass 16 kDa displayed several properties, including ability to bind 45Ca2+, that are characteristic of the regulatory (B) subunit of mammalian calcineurin and was recognized by an antiserum raised against bovine calcineurin. These antibodies were used to isolate the structural gene (CNB1) encoding this protein from a yeast expression library in the vector lambda gt11. The nucleotide sequence of CNB1 predicted a polypeptide similar in length and highly related in amino acid sequence (56% identity) to the mammalian calcineurin B subunit. Like its counterpart in higher cells, yeast Cnb1p was myristoylated at its N terminus. Mutants lacking Cnb1p, or all three calcineurin subunits (Cna1p, Cna2p, and Cnb1p), were viable. Extracts of cnb1 delta mutants contained no detectable calcineurin activity, even though Cna1p and Cna2p were present at normal levels, suggesting that the B subunit is required for full enzymatic activity in vitro. As was observed previously for MATa cna1 cna2 double mutants, MATa cnb1 mutants were defective in their ability to recover from alpha-factor-induced growth arrest. Thus, the B subunit also is required for the function of calcineurin in promoting adaptation of haploid yeast cells to pheromone in vivo.
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Dissertations / Theses on the topic "Calcineurine B-like"

1

Carrière, Cathelène. "Caractérisation des structures et fonctions de la phosphorylase kinase." Paris 6, 2008. http://www.theses.fr/2008PA066419.

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La phosphorylase kinase (PhK), enzyme clé de la glycogénolyse, est un complexe hexadécamérique formé de quatre sous-unités différentes (alpha, beta, gamma, delta)4. L’activité catalytique portée par la PhK gamma est modifiée par l’action des sous-unités apparentées alpha et beta (4/5 de la masse de l’enzyme). Des mutations dans la PhK conduisent à une maladie de stockage du glycogène (GSD) de type IX, le désordre le plus répandu dans le métabolisme du glycogène. Peu de choses sont connues sur la structure de l’holoenzyme et sur celle des sous-unités de la PhK (exception faite du domaine catalytique de la PhK gamma et de la PhK delta (calmoduline)). Dans cette thèse, nous avons utilisé des méthodes d’analyse de séquences pour révéler des caractéristiques structurales et fonctionnelles des sous-unités alpha et beta. Nous avons ainsi confirmé l’appartenance du premier domaine (A) à la famille des glucoamylases (Glycosyl Hydrolase 15) et montré que les domaines C et D sont reliés aux protéines « calcineurin B-like », membres de la famille EF-hand impliqués dans la régulation calcium-dépendante de kinases. La plupart des mutations faux-sens affectant la PhK alpha et conduisant à une déficience en PhK sont situées dans les sites actifs de ces domaines, suggérant qu’elles pourraient avoir un impact direct sur leurs fonctions. Par ailleurs, nous avons recalé dans le volume obtenu par cryo-microscopie électronique (résolution 9. 9 Angstrom) les structures 3D des différents domaines de la PhK en nous aidant des contraintes décrites dans la littérature. L’ensemble de ces résultats ouvre de nouvelles perspectives pour comprendre comment les sous-unités de la PhK régulent son activité
Phosphorylase kinase (PhK) is a key enzyme in glycogenolysis. PhK is a hexadecameric complex, made of four different subunits (alpha, beta, gamma, delta)4. Catalytic activity is conferred by the gamma subunit and is modified by the two related regulatory subunits alpha and beta which together account for ~ 4/5 of the PhK mass. Mutations in PhK lead to Glycogen Storage Disease (GSD) type IX, which is the most frequently encountered disorder of glycogen metabolism. The structural features of the quaternary structure of the holoenzyme and the PhK subunits, except for the catalytic domain of the PhK gamma and the PhK delta subunit are poorly understood. Here we have used sensitive methods of sequence analysis to unravel hidden structural and functional features of the PhK alpha and beta subunits. We confirm that the first domain (A) belongs to the glucoamylase family (Glycosyl Hydrolase 15) and show domains C and D are related to calcineurin B-like proteins, which are EF-hand family members involved in the Ca2+-dependent regulation of kinases. Mutations leading PhK deficiency, mostly missense mutations in PhK alpha, are located within the predicted active sites of these domains, suggesting that they may have a direct impact on their predicted functions. Furthermore, we docked the 3D structures of the different PhK domains into the volume obtained by cryo-electron microscopy at 9. 9 Angstrom resolution constraining with various interaction data reported in the literature. Altogether, our findings open new perspectives to understand how the different PhK subunits may regulate the holoenzyme activity
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2

Taylor, John Philip. "Sub-cellular localisation and function of calcineurin B-like proteins in plant cells." Thesis, University of East Anglia, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.268512.

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Yen, Tzu Chuan. "The Role of Calcineurin B-Like 10 in Flowers During Growth in Saline Conditions." Thesis, The University of Arizona, 2014. http://hdl.handle.net/10150/322094.

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4

Kim, Yongsig. "Characterization of the Arabidopsis Calcineurin B-like Calcium Sensors in Environmental and Developmental Signal Transduction." Diss., The University of Arizona, 2006. http://hdl.handle.net/10150/193680.

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In plants, the regulatory networks that have evolved to generate the appropriate cellular responses to external and internal stimuli often include a transient increase in intracellular calcium (Ca²⁺). One ten member, plant-specific family of Ca²⁺ sensing elements, the calcineurin B-like (CBL) protein family, is thought to relay the Ca²⁺ signal to downstream targets when plants experience an abiotic stress. The purpose of this study was to uncover critical functions of four CBL proteins. CBL10 was chosen for its distinct amino acid sequence and unique genomic structure among the CBL proteins. CBL1 and CBL9, generated by segmental duplication, were chosen based on their high level of amino acid identity. CBL8 was chosen based on its sequence and genomic structure similarities to SOS3/CBL4, the founding member of the CBL family. An Arabidopsis CBL10 knock-out insertion, cbl10-1, was isolated and found to have reduced stamen elongation, leading to male sterility. The mutant also showed growth arrest in aerial portions of the plant and developed chlorosis in response to increasing salt concentrations. Alternative pre-mRNA splicing generated five CBL10.2 variants whose transcript levels were regulated by cold or salt treatment, suggesting that CBL10 is involved in normal development and plant growth during abiotic stress via tight regulation of transcript levels. Phylogenetic analysis suggests that CBL1 and CBL9 may compensate for each other in the regulation of essential functions in the single mutant backgrounds. To investigate the crucial functions of these genes, a cbl1 cbl9 double mutant was generated. When grown under drought conditions, the double mutant was less sensitive to ABA, lost more water and produced more shriveled seeds than wild-type plants suggesting that both CBL1 and CBL9 play key roles in relaying drought stress signals during vegetative and reproductive growth. Because phylogenetic analysis and amino acid sequence comparisons suggest that CBL8 may function redundantly with SOS3/CBL4, a cbl4 cbl8 double mutant was generated. The cbl4 cbl8 double mutant phenocopied the sos3-1 (cbl4) mutant during salt and ABA treatments. CBL8 promoter activity in accessory cells of trichomes and root hairs suggests that CBL8 may have a function in development of these specialized epidermal cells.
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Ijato, Toyosi [Verfasser], and Uwe [Akademischer Betreuer] Ludewig. "Understanding the role of the Calcineurin B-like (CBL) proteins and the CBL-Interacting Protein Kinases (CIPK) of wheat (Triticum aestivum) in the regulation of its high affinity ammonium transporters / Toyosi Ijato ; Betreuer: Uwe Ludewig." Hohenheim : Kommunikations-, Informations- und Medienzentrum der Universität Hohenheim, 2021. http://d-nb.info/1233353195/34.

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Hou, Yueh-Ju, and 侯玥如. "Roles of Calcineurin B-Like proteins (CBLs) and F-box genes in nitrate signaling." Thesis, 2008. http://ndltd.ncl.edu.tw/handle/81488410452410155706.

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碩士
國立陽明大學
生命科學暨基因體科學研究所
96
Nitrate is not only a macronutrient but also acts as a signal molecule on regulating gene expression and root growth. Nitrate-induced rapid genes expression is referred as primary nitrate response. Little is known to be involved in nitrate signaling. In this study, signaling component genes from microarray data, two Calcineurin B-Like (CBL) and two F-box genes, were evaluated for their potential roles in nitrate signaling. Previous study has shown that CBL-interacting protein kinase 8 (CIPK8) and CIPK23 was found to regulate primary nitrate response and nitrate-modulated primary root growth. Once signal perceived, CBLs directly activate CIPKs to trigger downstream response. Since CBL1 and CBL9 interact with CIPK8 and CIPK23, suggesting that these two CBLs may be involved in nitrate signaling. In this study, Q-PCR analysis showed that CBL1 and CBL9 were nitrate-inducible genes. The induction levels of primary nitrate response marker genes, nitrate transporters CHL1 and NRT2.1, were reduced in cbl1 and cbl9 mutants. However, the reduced expressions observed in single mutants were recovered in cbl1cbl9 double mutant. Yeast two-hybrid assay showed that CBL1 and CBL9 interacted with C-terminal region of CHL1. Xenopus oocyte uptake assay further revealed that CHL1 uptake activity was reduced while co-expressed with CBL1 and CHL1, implying that CBL1 might involved in modulation uptake ability or protein stability of CHL1. Furthermore, the cbl1cbl9, but not single mutants, displayed defect in primary root growth, indicating that CBL1 and CBL9 were redundant in regulating nitrate-mediated primary root growth. Taken together, this study showed that CBL1 and CBL9 played multiple roles in nitrate signaling. Previous studies show that F-box genes participate in several plant signaling transduction such as hormone and light response. Although AFB3 and FBL6 were nitrate-inducible genes, the expressions of primary nitrate response genes and protein level of CHL1 were not significantly altered in afb3 and fbl6 mutants. Moreover, the primary root length of wild-type, afb3 and fbl6 were similar in nitrate medium. These results suggested that AFB3 and FBL6 might be involved in other unknown nitrate signaling pathway.
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