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Journal articles on the topic 'Calcineurine B-like'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Shi, Jinrui, Kyung-Nam Kim, Olga Ritz, Veronica Albrecht, Rajeev Gupta, Klaus Harter, Sheng Luan, and Jorg Kudla. "Novel Protein Kinases Associated with Calcineurin B-Like Calcium Sensors in Arabidopsis." Plant Cell 11, no. 12 (December 1999): 2393. http://dx.doi.org/10.2307/3870963.

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12

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 (CBLP)." Japanese Journal of Pharmacology 58 (1992): 325. http://dx.doi.org/10.1016/s0021-5198(19)49470-5.

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13

Shi, Jinrui, Kyung-Nam Kim, Olga Ritz, Veronica Albrecht, Rajeev Gupta, Klaus Harter, Sheng Luan, and Jörg Kudla. "Novel Protein Kinases Associated with Calcineurin B–like Calcium Sensors in Arabidopsis." Plant Cell 11, no. 12 (December 1999): 2393–405. http://dx.doi.org/10.1105/tpc.11.12.2393.

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14

Liu, Li-Li, Hui-Min Ren, Li-Qing Chen, Yi Wang, and Wei-Hua Wu. "A Protein Kinase, Calcineurin B-Like Protein-Interacting Protein Kinase9, Interacts with Calcium Sensor Calcineurin B-Like Protein3 and Regulates Potassium Homeostasis under Low-Potassium Stress in Arabidopsis." Plant Physiology 161, no. 1 (October 29, 2012): 266–77. http://dx.doi.org/10.1104/pp.112.206896.

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15

Tominaga, Misumi, Akiko Harada, Toshinori Kinoshita, and Ken-ichiro Shimazaki. "Biochemical Characterization of Calcineurin B-Like-Interacting Protein Kinase in Vicia Guard Cells." Plant and Cell Physiology 51, no. 3 (January 7, 2010): 408–21. http://dx.doi.org/10.1093/pcp/pcq006.

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16

MA, Bo-jun, Zhi-min GU, Hai-juan TANG, Xi-feng CHEN, Feng LIU, and Hong-sheng ZHANG. "Preliminary Study on Function of Calcineurin B-Like Protein Gene OsCBL8 in Rice." Rice Science 17, no. 1 (March 2010): 10–18. http://dx.doi.org/10.1016/s1672-6308(08)60099-2.

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17

Chen, Xunji, Guo Chen, Jianping Li, Xiaoyan Hao, Zumuremu Tuerxun, Xiaochun Chang, Shengqi Gao, and Quansheng Huang. "A maize calcineurin B‐like interacting protein kinase ZmCIPK42 confers salt stress tolerance." Physiologia Plantarum 171, no. 1 (November 8, 2020): 161–72. http://dx.doi.org/10.1111/ppl.13244.

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18

Kim, Kyung-Nam, Yong Hwa Cheong, Rajeev Gupta, and Sheng Luan. "Interaction Specificity of Arabidopsis Calcineurin B-Like Calcium Sensors and Their Target Kinases." Plant Physiology 124, no. 4 (December 1, 2000): 1844–53. http://dx.doi.org/10.1104/pp.124.4.1844.

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19

Dong, Lianhong, Qian Wang, S. M. Nuruzzaman Manik, Yufeng Song, Sujuan Shi, Yulong Su, Guanshan Liu, and Haobao Liu. "Nicotiana sylvestris calcineurin B-like protein NsylCBL10 enhances salt tolerance in transgenic Arabidopsis." Plant Cell Reports 34, no. 12 (August 30, 2015): 2053–63. http://dx.doi.org/10.1007/s00299-015-1851-4.

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20

Withee, James L., Romita Sen, and Martha S. Cyert. "Ion Tolerance of Saccharomyces cerevisiae Lacking the Ca2+/CaM-Dependent Phosphatase (Calcineurin) Is Improved by Mutations in URE2 or PMA1." Genetics 149, no. 2 (June 1, 1998): 865–78. http://dx.doi.org/10.1093/genetics/149.2.865.

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Abstract Calcineurin is a conserved, Ca2+/CaM-stimulated protein phosphatase required for Ca2+-dependent signaling in many cell types. In yeast, calcineurin is essential for growth in high concentrations of Na+, Li+, Mn2+, and OH−, and for maintaining viability during prolonged treatment with mating pheromone. In contrast, the growth of calcineurin-mutant yeast is better than that of wild-type cells in the presence of high concentrations of Ca2+. We identified mutations that suppress multiple growth defects of calcineurin-deficient yeast (cnb1Δ or cna1Δ cna2Δ). Mutations in URE2 suppress the sensitivity of calcineurin mutants to Na+, Li+, and Mn2+, and increase their survival during treatment with mating pheromone. ure2 mutations require both the transcription factor Gln3p and the Na+ ATPase Pmr2p to confer Na+ and Li+ tolerance. Mutations in PMA1, which encodes the yeast plasma membrane H+-ATPase, also suppress many growth defects of calcineurin mutants. pma1 mutants display growth phenotypes that are opposite to those of calcineurin mutants; they are resistant to Na+, Li+, and Mn2+, and sensitive to Ca2+. We also show that calcineurin mutants are sensitive to aminoglycoside antibiotics such as hygromycin B while pma1 mutants are more resistant than wild type. Furthermore, pma1 and calcineurin mutations have antagonistic effects on intracellular [Na+] and [Ca2+]. Finally, we show that yeast expressing a constitutively active allele of calcineurin display pma1-like phenotypes, and that membranes from these yeast have decreased levels of Pma1p activity. These studies further characterize the roles that URE2 and PMA1 play in regulating intracellular ion homeostasis.

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21

Kurusu, Takamitsu, Jumpei Hamada, Haruyasu Hamada, Shigeru Hanamata, and Kazuyuki Kuchitsu. "Roles of calcineurin B-like protein-interacting protein kinases in innate immunity in rice." Plant Signaling & Behavior 5, no. 8 (August 2010): 1045–47. http://dx.doi.org/10.4161/psb.5.8.12407.

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22

Wu, Wu, Qing Chen, Feng Geng, Li Tong, Rui Yang, Jinju Yang, Hongwei Zhang, Zongchao Jia, and Qun Wei. "Calcineurin B stimulates cytokine production through a CD14‐independent Toll‐like receptor 4 pathway." Immunology & Cell Biology 94, no. 3 (November 17, 2015): 285–92. http://dx.doi.org/10.1038/icb.2015.91.

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23

Kabir, Mohammad Humayun. "Response of Calcineurin B-like Protein Kinase Gene in Tomato to Various Abiotic Stresses." Journal of the Korean Society for Applied Biological Chemistry 53, no. 1 (February 2009): 15–21. http://dx.doi.org/10.3839/jksabc.2010.003.

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24

Carrière, Cathelène, Jean-Paul Mornon, Catherine Venien-Bryan, Nicolas Boisset, and Isabelle Callebaut. "Calcineurin B-like domains in the large regulatory α/β subunits of phosphorylase kinase." Proteins: Structure, Function, and Bioinformatics 71, no. 4 (March 4, 2008): 1597–606. http://dx.doi.org/10.1002/prot.22006.

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25

Kudla, J., Q. Xu, K. Harter, W. Gruissem, and S. Luan. "Genes for calcineurin B-like proteins in Arabidopsis are differentially regulated by stress signals." Proceedings of the National Academy of Sciences 96, no. 8 (April 13, 1999): 4718–23. http://dx.doi.org/10.1073/pnas.96.8.4718.

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26

Giong, Hoi-Khoanh, Sunok Moon, and Ki-Hong Jung. "A systematic view of the rice calcineurin B-like protein interacting protein kinase family." Genes & Genomics 37, no. 1 (October 15, 2014): 55–68. http://dx.doi.org/10.1007/s13258-014-0229-2.

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27

Wang, Maoyan, Dan Gu, Tingsong Liu, Zhaoqiang Wang, Xiying Guo, Wei Hou, Yunfeng Bai, Xiaoping Chen, and Guoying Wang. "Overexpression of a putative maize calcineurin B-like protein in Arabidopsis confers salt tolerance." Plant Molecular Biology 65, no. 6 (September 20, 2007): 733–46. http://dx.doi.org/10.1007/s11103-007-9238-8.

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28

Kumar, Manoj, Komal Sharma, Akhilesh K. Yadav, Kajal Kanchan, Madhu Baghel, Suneel Kateriya, and Girdhar K. Pandey. "Genome-wide identification and biochemical characterization of calcineurin B-like calcium sensor proteins in Chlamydomonas reinhardtii." Biochemical Journal 477, no. 10 (May 28, 2020): 1879–92. http://dx.doi.org/10.1042/bcj20190960.

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Calcium (Ca2+) signaling is involved in the regulation of diverse biological functions through association with several proteins that enable them to respond to abiotic and biotic stresses. Though Ca2+-dependent signaling has been implicated in the regulation of several physiological processes in Chlamydomonas reinhardtii, Ca2+ sensor proteins are not characterized completely. C. reinhardtii has diverged from land plants lineage, but shares many common genes with animals, particularly those encoding proteins of the eukaryotic flagellum (or cilium) along with the basal body. Calcineurin, a Ca2+/calmodulin-dependent protein phosphatase, is an important effector of Ca2+ signaling in animals, while calcineurin B-like proteins (CBLs) play an important role in Ca2+ sensing and signaling in plants. The present study led to the identification of 13 novel CBL-like Ca2+ sensors in C. reinhardtii genome. One of the archetypical genes of the newly identified candidate, CrCBL-like1 was characterized. The ability of CrCBL-like1 protein to sense as well as bind Ca2+ were validated using two-step Ca2+-binding kinetics. The CrCBL-like1 protein localized around the plasma membrane, basal bodies and in flagella, and interacted with voltage-gated Ca2+ channel protein present abundantly in the flagella, indicating its involvement in the regulation of the Ca2+ concentration for flagellar movement. The CrCBL-like1 transcript and protein expression were also found to respond to abiotic stresses, suggesting its involvement in diverse physiological processes. Thus, the present study identifies novel Ca2+ sensors and sheds light on key players involved in Ca2+signaling in C. reinhardtii, which could further be extrapolated to understand the evolution of Ca2+ mediated signaling in other eukaryotes.

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29

Yang, Yang, Chi Zhang, Ren-Jie Tang, Hai-Xia Xu, Wen-Zhi Lan, Fugeng Zhao, and Sheng Luan. "Calcineurin B-Like Proteins CBL4 and CBL10 Mediate Two Independent Salt Tolerance Pathways in Arabidopsis." International Journal of Molecular Sciences 20, no. 10 (May 16, 2019): 2421. http://dx.doi.org/10.3390/ijms20102421.

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In Arabidopsis, the salt overly sensitive (SOS) pathway, consisting of calcineurin B-like protein 4 (CBL4/SOS3), CBL-interacting protein kinase 24 (CIPK24/SOS2) and SOS1, has been well defined as a crucial mechanism to control cellular ion homoeostasis by extruding Na+ to the extracellular space, thus conferring salt tolerance in plants. CBL10 also plays a critical role in salt tolerance possibly by the activation of Na+ compartmentation into the vacuole. However, the functional relationship of the SOS and CBL10-regulated processes remains unclear. Here, we analyzed the genetic interaction between CBL4 and CBL10 and found that the cbl4 cbl10 double mutant was dramatically more sensitive to salt as compared to the cbl4 and cbl10 single mutants, suggesting that CBL4 and CBL10 each directs a different salt-tolerance pathway. Furthermore, the cbl4 cbl10 and cipk24 cbl10 double mutants were more sensitive than the cipk24 single mutant, suggesting that CBL10 directs a process involving CIPK24 and other partners different from the SOS pathway. Although the cbl4 cbl10, cipk24 cbl10, and sos1 cbl10 double mutants showed comparable salt-sensitive phenotype to sos1 at the whole plant level, they all accumulated much lower Na+ as compared to sos1 under high salt conditions, suggesting that CBL10 regulates additional unknown transport processes that play distinct roles from the SOS1 in Na+ homeostasis.

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30

Yadav, Akhilesh K., Saroj K. Jha, Sibaji K. Sanyal, Sheng Luan, and Girdhar K. Pandey. "Arabidopsis calcineurin B-like proteins differentially regulate phosphorylation activity of CBL-interacting protein kinase 9." Biochemical Journal 475, no. 16 (August 29, 2018): 2621–36. http://dx.doi.org/10.1042/bcj20180372.

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Calcium (Ca2+) is a versatile and ubiquitous second messenger in all eukaryotes including plants. In response to various stimuli, cytosolic calcium concentration ([Ca2+]cyt) is increased, leading to activation of Ca2+ sensors including Arabidopsis calcineurin B-like proteins (CBLs). CBLs interact with CBL-interacting protein kinases (CIPKs) to form CBL–CIPK complexes and transduce the signal downstream in the signalling pathway. Although there are many reports on the regulation of downstream targets by CBL–CIPK module, knowledge about the regulation of upstream components by individual CIPKs is inadequate. In the present study, we have carried out a detailed biochemical characterization of CIPK9, a known regulator of K+ deficiency in Arabidopsis, with its interacting CBLs. The present study suggests that CIPK9 specifically interacts with four CBLs, i.e. CBL1, CBL2, CBL3 and CBL9, in yeast two-hybrid assays. Out of these four CBLs, CBL2 and CBL3, specifically enhance the kinase activity of CIPK9, while the CBL1 and CBL9 decrease it as examined by in vitro kinase assays. In contrast, truncated CIPK9 (CIPK9ΔR), without the CBL-interacting regulatory C-terminal region, is not differentially activated by interacting CBLs. The protein phosphorylation assay revealed that CBL2 and CBL3 serve as preferred substrates of CIPK9. CBL2– and CBL3–CIPK9 complexes show altered requirement for metal cofactors when compared with CIPK9 alone. Moreover, the autophosphorylation of constitutively active CIPK9 (CIPK9T178D) and less active CIPK9 (CIPK9T178A) in the presence of CBL2 and CBL3 was further enhanced. Our study suggests that CIPK9 differentially phosphorylates interacting CBLs, and furthermore, the kinase activity of CIPK9 is also differentially regulated by specific interacting CBLs.

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31

Pandey, Girdhar K., Yong Hwa Cheong, Kyung-Nam Kim, John J. Grant, Legong Li, Wendy Hung, Cecilia D'Angelo, Stefan Weinl, Jörg Kudla, and Sheng Luan. "The Calcium Sensor Calcineurin B-Like 9 Modulates Abscisic Acid Sensitivity and Biosynthesis in Arabidopsis." Plant Cell 16, no. 7 (June 18, 2004): 1912–24. http://dx.doi.org/10.1105/tpc.021311.

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32

Ren, Xiao-Ling, Guo-Ning Qi, Han-Qian Feng, Shuai Zhao, Shuang-Shuang Zhao, Yi Wang, and Wei-Hua Wu. "Calcineurin B-like protein CBL10 directly interacts with AKT1 and modulates K+homeostasis in Arabidopsis." Plant Journal 74, no. 2 (February 13, 2013): 258–66. http://dx.doi.org/10.1111/tpj.12123.

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33

Greenblatt, Matthew B., Antonios Aliprantis, Bella Hu, and Laurie H. Glimcher. "Calcineurin regulates innate antifungal immunity in neutrophils." Journal of Experimental Medicine 207, no. 5 (April 26, 2010): 923–31. http://dx.doi.org/10.1084/jem.20092531.

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Patients taking immunosuppressive drugs, like cyclosporine A (CsA), that inhibit calcineurin are highly susceptible to disseminated fungal infections, although it is unclear how these drugs suppress resistance to these opportunistic pathogens. We show that in a mouse model of disseminated Candida albicans infection, CsA-induced susceptibility to fungal infection maps to the innate immune system. To further define the cell types targeted by CsA, we generated mice with a conditional deletion of calcineurin B (CnB) in neutrophils. These mice displayed markedly decreased resistance to infection with C. albicans, and both CnB-deficient and CsA-treated neutrophils showed a defect in the ex vivo killing of C. albicans. In response to the fungal-derived pathogen-associated molecular pattern zymosan, neutrophils lacking CnB displayed impaired up-regulation of genes (IL-10, Cox2, Egr1, and Egr2) regulated by nuclear factor of activated T cells, the best characterized CnB substrate. This activity was Myd88 independent and was reproduced by stimulation with the β(1,3) glucan curdlan, indicating that dectin-1, rather than toll-like receptors, is the upstream activator of calcineurin. Our results suggest that disseminated fungal infections seen in CsA-treated patients are not just a general consequence of systemic suppression of adaptive immunity but are, rather, a result of the specific blockade of evolutionarily conserved innate pathways for fungal resistance.

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34

Xu, Ling, Dayong Zhang, Zhaolong Xu, Yihong Huang, Xiaolan He, Jinyan Wang, Minfeng Gu, Jianbin Li, and Hongbo Shao. "Comparative expression analysis of Calcineurin B-like family gene CBL10A between salt-tolerant and salt-sensitive cultivars in B. oleracea." Science of The Total Environment 571 (November 2016): 1–10. http://dx.doi.org/10.1016/j.scitotenv.2016.07.130.

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35

Ok, Sung Han, Joo Hyuk Cho, Seung-Ick Oh, Mi Na Choi, Jae-Yeon Ma, Jeong-Sheop Shin, and Kyung-Nam Kim. "Calcineurin B-like 3 calcium sensor associates with and inhibits 5′-methylthioadenosine nucleosidase 2 in Arabidopsis." Plant Science 238 (September 2015): 228–40. http://dx.doi.org/10.1016/j.plantsci.2015.06.016.

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36

Shang, Guijun, Huaixing Cang, Zhijie Liu, Wei Gao, and Ruchang Bi. "Crystallization and preliminary crystallographic analysis of a calcineurin B-like protein 1 (CBL1) mutant fromAmmopiptanthus mongolicus." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 12 (November 25, 2010): 1602–5. http://dx.doi.org/10.1107/s1744309110039667.

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Kabir, M. H., and M. H. Wang. "Stress-induced expression profiling of a calcium sensor, calcineurin B-like protein gene (SlCBL) in tomato." Journal of Horticultural Science and Biotechnology 85, no. 2 (January 2010): 154–60. http://dx.doi.org/10.1080/14620316.2010.11512647.

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Pandey, Girdhar K., Poonam Kanwar, Amarjeet Singh, Leonie Steinhorst, Amita Pandey, Akhlilesh K. Yadav, Indu Tokas, et al. "Calcineurin B-Like Protein-Interacting Protein Kinase CIPK21 Regulates Osmotic and Salt Stress Responses in Arabidopsis." Plant Physiology 169, no. 1 (July 21, 2015): 780–92. http://dx.doi.org/10.1104/pp.15.00623.

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Li, D. D., X. L. Xia, W. L. Yin, and H. C. Zhang. "Two poplar calcineurin B-like proteins confer enhanced tolerance to abiotic stresses in transgenic Arabidopsis thaliana." Biologia plantarum 57, no. 1 (March 1, 2013): 70–78. http://dx.doi.org/10.1007/s10535-012-0251-7.

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Xu, Jiang, Hao-Dong Li, Li-Qing Chen, Yi Wang, Li-Li Liu, Liu He, and Wei-Hua Wu. "A Protein Kinase, Interacting with Two Calcineurin B-like Proteins, Regulates K+ Transporter AKT1 in Arabidopsis." Cell 125, no. 7 (June 2006): 1347–60. http://dx.doi.org/10.1016/j.cell.2006.06.011.

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Tuteja, Narendra, and Shilpi Mahajan. "Further Characterization of Calcineurin B-Like Protein and Its Interacting Partner CBL-Interacting Protein Kinase fromPisum sativum." Plant Signaling & Behavior 2, no. 5 (September 2007): 358–61. http://dx.doi.org/10.4161/psb.2.5.4178.

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Jung, Hee-Jeong, Md Abdul Kayum, Senthil Kumar Thamilarasan, Ujjal Kumar Nath, Jong-In Park, Mi-Young Chung, Yoonkang Hur, and Ill-Sup Nou. "Molecular characterisation and expression profiling of calcineurin B-like (CBL) genes in Chinese cabbage under abiotic stresses." Functional Plant Biology 44, no. 7 (2017): 739. http://dx.doi.org/10.1071/fp16437.

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Abstract:

Calcium signals act as a second messenger in plant responses to various abiotic stresses, which regulate a range of physiological processes. Calcium-binding proteins, like calcineurin B-like (CBL) proteins, belong to a unique group of calcium sensors that play a role in calcium signalling. However, their identities and functions are unknown in Chinese cabbage. In this study, 17 CBL genes were identified from the Brassica rapa L. (Chinese cabbage) database and Br135K microarray datasets. They were used to construct a phylogenetic tree with known CBL proteins of other species. Analysis of genomic distribution and evolution revealed different gene duplication in Chinese cabbage compared to Arabidopsis. The microarray expression analysis showed differential expression of BrCBL genes at various temperatures. Organ-specific expression was observed by RT–PCR, and qRT–PCR analyses revealed responsiveness of BrCBL genes to cold, drought and salt stresses. Our findings confirm that CBL genes are involved in calcium signalling and regulate responses to environmental stimuli, suggesting this family gene have crucial role to play in plant responses to abiotic stresses. The results facilitate selection of candidate genes for further functional characterisation. In addition, abiotic stress-responsive genes reported in this study might be exploited for marker-aided backcrossing of Chinese cabbage.

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Su, Wei, Jiaxue Wu, Chun Wei, Kegui Li, Guangming He, Kotb Attla, Xiaoyin Qian, and Jinshui Yang. "Interaction between programmed cell death 5 and calcineurin B-like interacting protein kinase 23 in Oryza sativa." Plant Science 170, no. 6 (June 2006): 1150–55. http://dx.doi.org/10.1016/j.plantsci.2006.02.003.

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Gao, Yuanlin, and Guozeng Zhang. "A calcium sensor calcineurin B-like 9 negatively regulates cold tolerance via calcium signaling in Arabidopsis thaliana." Plant Signaling & Behavior 14, no. 3 (January 29, 2019): e1573099. http://dx.doi.org/10.1080/15592324.2019.1573099.

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Tang, Wei, and Wells A. Thompson. "Role of the Arabidopsis calcineurin B-like protein-interacting protein kinase CIPK21 in plant cold stress tolerance." Plant Biotechnology Reports 14, no. 3 (January 24, 2020): 275–91. http://dx.doi.org/10.1007/s11816-020-00597-7.

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Gu, Zhimin, Bojun Ma, Yan Jiang, Zhiwei Chen, Xuan Su, and Hongsheng Zhang. "Expression analysis of the calcineurin B-like gene family in rice (Oryza sativa L.) under environmental stresses." Gene 415, no. 1-2 (May 2008): 1–12. http://dx.doi.org/10.1016/j.gene.2008.02.011.

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Matsumoto, M., Y. Miyake, M. Nagita, H. Inoue, D. Shitakubo, K. Takemoto, C. Ohtsuka, H. Murakami, N. Nakamura, and H. Kanazawa. "A Serine/Threonine Kinase Which Causes Apoptosis-Like Cell Death Interacts with a Calcineurin B-Like Protein Capable of Binding Na+/H+ Exchanger." Journal of Biochemistry 130, no. 2 (August 1, 2001): 217–25. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a002975.

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Egea, Isabel, Benito Pineda, Ana Ortíz-Atienza, Félix A. Plasencia, Stéphanie Drevensek, Begoña García-Sogo, Fernando J. Yuste-Lisbona, et al. "The SlCBL10 Calcineurin B-Like Protein Ensures Plant Growth under Salt Stress by Regulating Na+ and Ca2+ Homeostasis." Plant Physiology 176, no. 2 (December 11, 2017): 1676–93. http://dx.doi.org/10.1104/pp.17.01605.

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Ketehouli, Toi, Yong-Gang Zhou, Si-Yu Dai, Kue Foka Idrice Carther, Da-Qian Sun, Yang Li, Quoc Viet Hoang Nguyen, et al. "A soybean calcineurin B-like protein-interacting protein kinase, GmPKS4, regulates plant responses to salt and alkali stresses." Journal of Plant Physiology 256 (January 2021): 153331. http://dx.doi.org/10.1016/j.jplph.2020.153331.

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Oh, Seung-Ick, Jimyeong Park, Sunhee Yoon, Yungyeong Kim, Soojin Park, Migyeong Ryu, Min Jung Nam, et al. "The Arabidopsis Calcium Sensor Calcineurin B-Like 3 Inhibits the 5′-Methylthioadenosine Nucleosidase in a Calcium-Dependent Manner." Plant Physiology 148, no. 4 (October 22, 2008): 1883–96. http://dx.doi.org/10.1104/pp.108.130419.

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