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Journal articles on the topic 'Protein kinasa'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Mattei, Jean Camille, Corinne Bouvier-Labit, Doriane Barets, Nicolas Macagno, Mathieu Chocry, Frédéric Chibon, Philippe Morando, et al. "Pan Aurora Kinase Inhibitor: A Promising Targeted-Therapy in Dedifferentiated Liposarcomas With Differential Efficiency Depending on Sarcoma Molecular Profile." Cancers 12, no. 3 (March 3, 2020): 583. http://dx.doi.org/10.3390/cancers12030583.

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Soft tissue sarcoma (STS) are rare and aggressive tumours. Their classification includes numerous histological subtypes of frequent poor prognosis. Liposarcomas (LPS) are the most frequent type among them, and the aggressiveness and deep localization of dedifferentiated LPS are linked to high levels of recurrence. Current treatments available today lead to five-year overall survival has remained stuck around 60–70% for the past three decades. Here, we highlight a correlation between Aurora kinasa A (AURKA) and AURKB mRNA overexpression and a low metastasis-free survival. AURKA and AURKB expression analysis at genomic and protein level on a 9-STS cell lines panel highlighted STS heterogeneity, especially in LPS subtype. AURKA and AURKB inhibition by RNAi and drug targeting with AMG 900, a pan Aurora Kinase inhibitor, in four LPS cell lines reduces cell survival and clonogenic proliferation, inducing apoptosis and polyploidy. When combined with doxorubicin, the standard treatment in STS, aurora kinases inhibitor can be considered as an enhancer of standard treatment or as an independent drug. Kinome analysis suggested its effect was linked to the inhibition of the MAP-kinase pathway, with differential drug resistance profiles depending on molecular characteristics of the tumor. Aurora Kinase inhibition by AMG 900 could be a promising therapy in STS.

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2

Pang, Kam-Lee, Wei-Li Thong, and Siew-Eng How. "Cinnamomum Iners as Mitogen-Activated Protein Kinase Kinase (MKK1) Inhibitor." International Journal of Engineering and Technology 1, no. 4 (2009): 310–13. http://dx.doi.org/10.7763/ijet.2009.v1.61.

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3

Guda, B. B., V. V. Pushkarev, O. V. Zhuravel, A. Ye Kovalenko, V. M. Pushkarev, Y. M. Taraschenko, and M. D. Tronko. "Protein kinase Akt activity in human thyroid tumors." Ukrainian Biochemical Journal 88, no. 5 (October 31, 2016): 90–95. http://dx.doi.org/10.15407/ubj88.05.090.

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4

Kim, Young-Sook. "A Protein Kinase-A Inhibitor, KT5720, Suppressed Cytopathic Effect Caused by Vesicular Stomatitis Virus." Journal of Life Science 17, no. 10 (October 30, 2007): 1361–67. http://dx.doi.org/10.5352/jls.2007.17.10.1361.

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5

Stolworthy, Tiffany S., and Margaret E. Black. "The mouse guanylate kinase double mutant E72Q/D103N is a functional adenylate kinase." Protein Engineering, Design and Selection 14, no. 11 (November 2001): 903–9. http://dx.doi.org/10.1093/protein/14.11.903.

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6

Moon, Il-Soo, and Dae-Hyun Seog. "Protein Kinase (PKC)-ε Interacts with the Serotonin Transporter (SERT) C-Terminal Region." Journal of Life Science 20, no. 10 (October 30, 2010): 1451–57. http://dx.doi.org/10.5352/jls.2010.20.10.1451.

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7

Edwards, Amelia S., and John D. Scott. "A-kinase anchoring proteins: protein kinase A and beyond." Current Opinion in Cell Biology 12, no. 2 (April 2000): 217–21. http://dx.doi.org/10.1016/s0955-0674(99)00085-x.

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8

Vallespí, Teresa, Mildred Borrego, Doulous Colomé, Ana Jaen, Maria Rozman, and Isabel Massagué. "Quantitative Polymerase Chain Reaction (qPCR) at Diagnosis and Follow-Up of Patients with Chronic Myeloid Leukemia in Treatment with Imatinib." Blood 104, no. 11 (November 16, 2004): 4688. http://dx.doi.org/10.1182/blood.v104.11.4688.4688.

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Abstract Imatinib, a selective inhibitor of tyrosin-kinasa BCR/ABL fusion protein, produces high response rates in patients with chronic myeloid leukemia (CML) in the chronic phase. The behavior of the levels of the BCR/ABL transcript by qPCR technique was studied in 24 patients (13M/11F; median age: 49.6 years, range: 23–73), diagnosed of CML in chronic phase, before and after the treatment with imatinib (at the 0, 3, 7, 11 and 15 months). Eight patients had previously received interferon alpha or busulphan and 16 hidroxiurea. The amplification of BCR/ABL with the qPCR technique, according to protocol BIOMED-2, was carried out in samples of bone marrow (n = 23) and peripheral blood (n = 48). Results were calculated in relation to a control gene of the glucuronidasa (GUS) and expressed in logarithmic scale (log10). Median time from the diagnosis was of 28 months and median treatment time with imatinib was 14 months. The median reduction of BCR/ABL transcripts was 1,98 log after three months and decreased further (2,71 log) during follow-up. Both of them were significative when compare with base line levels (P <0.001). The reduction was greater in patients who received a dose ³ 400 mg/day (n=16) than those with 300 mg/day (n=8). Three patients reached a major molecular response (ratio BCR-ABL/GUS <0.005) up to 15 months of treatment. In conclusion: the determination of the BCR/ABL transcripts by qPCR contributes with valuable information about the effect of imatinib in patients with CML. The logarithmic reduction is higher in the beginning of the treatment and doses ³ 400 mg/day are associated with a greater reduction of the tumoral load. Figure Figure

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9

Protopopov, M. V., O. V. Ostrynska, and D. H. Ivanchenko. "Developing of protein kinase CK2 inhibitors based on purine-2,6-diones derivatives." Ukrainian Biochemical Journal 89, no. 5 (October 25, 2017): 32–39. http://dx.doi.org/10.15407/ubj89.05.032.

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10

Tougard, Pierre, Thanh Hung Le, Philippe Minard, Michel Desmadril, Jeannine M. Yon, Thierry Bizebard, Gérard Lebras, and Christian Dumas. "Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala." "Protein Engineering, Design and Selection" 9, no. 2 (1996): 181–87. http://dx.doi.org/10.1093/protein/9.2.181.

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11

Yasuda, Jun, Alan J. Whitmarsh, Julie Cavanagh, Manoj Sharma, and Roger J. Davis. "The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins." Molecular and Cellular Biology 19, no. 10 (October 1, 1999): 7245–54. http://dx.doi.org/10.1128/mcb.19.10.7245.

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ABSTRACT Activation of the c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is mediated by a protein kinase cascade. This signaling mechanism may be coordinated by the interaction of components of the protein kinase cascade with scaffold proteins. The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates signaling by the mixed-lineage kinase (MLK)→MAP kinase kinase 7 (MKK7)→JNK pathway. The scaffold proteins JIP1 and JIP2 interact to form oligomeric complexes that accumulate in peripheral cytoplasmic projections extended at the cell surface. The JIP proteins function by aggregating components of a MAP kinase module (including MLK, MKK7, and JNK) and facilitate signal transmission by the protein kinase cascade.

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12

Jung, Hyun-Lyung, Young Ho Shin, and Ho-Youl Kang. "Effects of Endurance Exercise and Ginsenoside Rb1on AMP-Activated Protein Kinase, Phosphatidylinositol 3-Kinase Expression and Glucose Uptake in the Skeletal Muscle of Rats." Journal of the Korean Society of Food Science and Nutrition 42, no. 8 (August 31, 2013): 1197–203. http://dx.doi.org/10.3746/jkfn.2013.42.8.1197.

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13

Perrier, V., S. Burlacu-Miron, A. Boussac, A. Meier, and A. M. Gilles. "Metal chelating properties of adenylate kinase from Paracoccus denitrificans." Protein Engineering Design and Selection 11, no. 10 (October 1, 1998): 917–23. http://dx.doi.org/10.1093/protein/11.10.917.

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14

Nomiyama, Yoko, Mitsuo Tashiro, Taizo Yamaguchi, Shiro Watanabe, Masashi Taguchi, Hiroshi Asaumi, Hayato Nakamura, and Makoto Otsuki. "High glucose activates rat pancreatic stellate cells through protein kinase C and p38 mitogen-activated protein kinase pathway." Suizo 22, no. 5 (2007): 595–97. http://dx.doi.org/10.2958/suizo.22.595.

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15

Jung, Se-Hui, Deok-Hoon Kong, Hye-Yoon Jeon, Eun-Taek Han, Won Sun Park, Seok-Ho Hong, Young-Myeong Kim, and Kwon-Soo Ha. "Systematic investigation of protein kinase A substrate proteins using on-chip protein kinase kinetic profiling." Analyst 142, no. 12 (2017): 2239–46. http://dx.doi.org/10.1039/c6an02682f.

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An on-chip protein kinase assay for profiling kinase kinetic parameters by introducing the substrate affinity (K_m) and the phosphorylation rate (V_p) under physiological conditions.

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16

Qu, Yi, Joseph Torchia, Thanh Duc Phan, Po Hsiung Wu, and Amar Kumar Sen. "Endogenous substrates of rat heart protein kinase C type I, II, and III isozymic forms in cardiac sarcolemma." Biochemistry and Cell Biology 70, no. 1 (January 1, 1992): 81–85. http://dx.doi.org/10.1139/o92-012.

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The endogenous substrate proteins of rat cardiac protein kinase C type I, II, and III isozymic forms were studied in rat cardiac sarcolemma. The 19-, 21-, 29-, 35-, and 95-kDa proteins were phosphorylated by both types II and III, but not type I. The extent of phosphorylation by individual protein kinase C isozymic forms was additive and equal to the extent of phosphorylation observed when a mixture of isozymic forms was employed. The extent of phosphorylation of the 21-kDa protein by type III was much higher than that by type II. These results suggest that the protein kinase C isozymes have preferences for specific endogenous substrate proteins. The phosphorylation of these endogenous substrate proteins by protein kinase C isozymes probably plays a role in cardiac cell functions.Key words: cardiac sarcolemma, protein kinase C isozymes, phosphorylation, substrate proteins.

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17

Trojanek, Joanna B., Maria M. Klimecka, Anna Fraser, Grazyna Dobrowolska, and Grazyna Muszyńska. "Characterization of dual specificity protein kinase from maize seedlings." Acta Biochimica Polonica 51, no. 3 (September 30, 2004): 635–47. http://dx.doi.org/10.18388/abp.2004_3549.

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A protein kinase of 57 kDa, able to phosphorylate tyrosine in synthetic substrates pol(Glu4,Tyr1) and a fragment of Src tyrosine kinase, was isolated and partly purified from maize seedlings (Zea mays). The protein kinase was able to phosphorylate exogenous proteins: enolase, caseins, histones and myelin basic protein. Amino acid analysis of phosphorylated casein and enolase, as well as of phosphorylated endogenous proteins, showed that both Tyr and Ser residues were phosphorylated. Phosphotyrosine was also immunodetected in the 57 kDa protein fraction. In the protein fraction there are present 57 kDa protein kinase and enolase. This co-purification suggests that enolase can be an endogenous substrate of the kinase. The two proteins could be resolved by two-dimensional electrophoresis. Specific inhibitors of typical protein-tyrosine kinases had essentially no effect on the activity of the maize enzyme. Staurosporine, a nonspecific inhibitor of protein kinases, effectively inhibited the 57 kDa protein kinase. Also, poly L-lysine and heparin inhibited tyrosine phosphorylation by 57 kDa maize protein kinase. The substrate and inhibitor specificities of the 57 kDa maize protein kinase phosphorylating tyrosine indicate that it is a novel plant dual-specificity protein kinase.

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18

Alcobendas, R. M., C. Quintana, J. Arostegui, C. Udaondo, S. Murias Loza, and A. Remesal. "AB0994 NEW ALTERNATIVE IN THE TREATMENT OF PATIENT WITH MUTATION OF GEN LACC1." Annals of the Rheumatic Diseases 79, Suppl 1 (June 2020): 1790.2–1790. http://dx.doi.org/10.1136/annrheumdis-2020-eular.5555.

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Background:Few patients have been described in the literature with mutations in the Lacasa Domain containing one (LACC1) gene. Its clinical presentation usually associates sustained systemic inflammation associated with chronic polyarticular erosive arthritis. Until now, there have been multiple treatments described to try to control the disease, however, they are generally unsuccessful in the long term.Objectives:Describe the clinical course of a patient as well as the different treatments usedMethods:Clinical chart reviewResults:Female 18-year-old born from a consanguineous Moroccan couple. Mother, brother and sister with similar conditions. She started at 3 years with fever, anemia, intense elevation of acute phase reactants and symmetric polyarthritis (knees, elbows, carps, shoulders, hands and ankles). Subsequent whole exome sequencing identified c.128_129delGT mutation in the LACC1/FAMIN gene. During the course of her illness, she has received treatment with oral, intravenous and infiltrated corticosteroid, methotrexate and etanercept, without getting adequate control of the disease. In 2016, she started treatment with tocilizumab (8 mg / kg every two weeks), obtaining an acceptable control of the disease (requiring periodic infiltrations every 2-3 months due to persistent arthritis). Nonetheless, in April 2019, she consulted for clinical worsening of the arthritis and laboratory test (C reactive protein 99.7 mg / L, erythrosedimentation rate 53 mm / h, leukocytes 13,500/µL and neutrophils 10,930/µL). At that time, she discontinued therapy with tocilizumab and started tofacitinib 5 mg every 12 hours with good evolution. Since its introduction, it has not required joint infiltration again and the inflammatory parameters (persistently elevated previously) have normalized.Conclusion:The jak kinasa inhibitors may be a treatment option in those patients with bad response to conventional therapy.References:[1]Rabionet R, Remesal A, Mensa-Vilaró A, Murías S, Alcobendas R, González-Roca E, Ruiz-Ortiz E, Antón J, Iglesias E, Modesto C, Comas D, Puig A, Drechsel O, Ossowski S, Yagüe J, Merino R, Estivill X, Arostegui JI. Biallelic loss-of-function LACC1/FAMIN Mutations Presenting as Rheumatoid Factor-Negative Polyarticular Juvenile Idiopathic Arthritis. Sci Rep. 2019 Mar 14;9(1):4579Disclosure of Interests:None declared

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19

SEGURO, Katsuya, and Masao MOTOKI. "Enzymatic phosphorylation of soybean proteins by protein kinase." Agricultural and Biological Chemistry 53, no. 12 (1989): 3263–68. http://dx.doi.org/10.1271/bbb1961.53.3263.

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20

Testori, Alessandro, Charles S. T. Hii, Agnes Fournier, Leigh A. Burgoyne, and Andrew W. Murray. "DNA-binding proteins in protein kinase C preparations." Biochemical and Biophysical Research Communications 156, no. 1 (October 1988): 222–27. http://dx.doi.org/10.1016/s0006-291x(88)80828-3.

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21

Martin, Torsten, Rita Sharma, Claudia Sippel, Karin Waegemann, Jürgen Soll, and Ute C. Vothknecht. "A Protein Kinase Family inArabidopsisPhosphorylates Chloroplast Precursor Proteins." Journal of Biological Chemistry 281, no. 52 (November 7, 2006): 40216–23. http://dx.doi.org/10.1074/jbc.m606580200.

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22

Radau, Boris, Albrecht Otto, Eva-Christina Müller, and Peter Westermann. "Protein kinase Cα-dependent phosphorylation of Golgi proteins." Electrophoresis 21, no. 13 (July 1, 2000): 2684–87. http://dx.doi.org/10.1002/1522-2683(20000701)21:13<2684::aid-elps2684>3.0.co;2-g.

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23

Seguro, Katsuya, and Masao Motoki. "Enzymatic Phosphorylation of Soybean Proteins by Protein Kinase." Agricultural and Biological Chemistry 53, no. 12 (December 1989): 3263–68. http://dx.doi.org/10.1080/00021369.1989.10869851.

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24

Sihag, Ram K., Arco Y. Jeng, and Ralph A. Nixon. "Phosphorylation of neurofilament proteins by protein kinase C." FEBS Letters 233, no. 1 (June 6, 1988): 181–85. http://dx.doi.org/10.1016/0014-5793(88)81380-2.

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25

Moon, Il-Soo. "Expression of c-Jun N-Terminal Kinase (JNK)-Interacting Protein (JIP) in Cultured Rat Hippocampal Neurons." Journal of Life Science 17, no. 12 (December 30, 2007): 1627–33. http://dx.doi.org/10.5352/jls.2007.17.12.1627.

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26

Kim, Hyo Joon, Satoshi Nishikawa, Toshiki Tanaka, Seiichi Uesugi, Hitoshi Takenaka, Minoru Hamada, and Stephen A. Kuby. "Synthetic genes for human muscle-type adenylate kinase in Escherichia coli." "Protein Engineering, Design and Selection" 2, no. 5 (1989): 379–86. http://dx.doi.org/10.1093/protein/2.5.379.

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27

Ballery, Nathalie, Philippe Minard, Michel Desmadril, Jean-Michel Betton, David Perahia, Liliane Mouawad, Len Hall, and Jeannine M. Yon. "Introduction of internal cysteines as conformational probes in yeast phosphoglycerate kinase." "Protein Engineering, Design and Selection" 3, no. 3 (1990): 199–204. http://dx.doi.org/10.1093/protein/3.3.199.

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28

Pecorari, Frederic, Philippe Minard, Michel Desmadril, and Jeannine M. Yon. "Structure and functional complementation of engineered fragments from yeast phosphoglycerate kinase." "Protein Engineering, Design and Selection" 6, no. 3 (1993): 313–24. http://dx.doi.org/10.1093/protein/6.3.313.

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29

Pendergast, A. M., J. A. Traugh, and O. N. Witte. "Normal cellular and transformation-associated abl proteins share common sites for protein kinase C phosphorylation." Molecular and Cellular Biology 7, no. 12 (December 1987): 4280–89. http://dx.doi.org/10.1128/mcb.7.12.4280.

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Viral transduction and chromosomal translocations of the c-abl gene result in the synthesis of abl proteins with structurally altered amino termini. These altered forms of the abl protein, but not the c-abl proteins, are detectably phosphorylated on tyrosine in vivo. In contrast, all forms of the abl protein are phosphorylated on serine following in vivo labeling with Pi. Treatment of NIH-3T3 cells with protein kinase C activators resulted in a four- to eightfold increase in the phosphorylation of murine c-abl due to modification of two serines on the c-abl protein. Purified protein kinase C phosphorylated all abl proteins at the same two sites. Both sites are precisely conserved in murine and human abl proteins. The sites on the abl proteins were found near the carboxy terminus. In contrast, for the epidermal growth factor receptor (T. Hunter, N. Ling, and J. A. Cooper, Nature [London] 311:480-483, 1984) and pp60src (K. L. Gould, J. R. Woodgett, J. A. Cooper, J. E. Buss, D. Shalloway, and T. Hunter, Cell 42:849-857, 1985), the sites of protein kinase C phosphorylation are amino-terminal to the kinase domain. The abl carboxy-terminal region is not necessary for the tyrosine kinase activity or transformation potential of the viral abl protein and may represent a regulatory domain. Using an in vitro immune complex kinase assay, we were not able to correlate reproducible changes in c-abl activity with phosphorylation by protein kinase C. However, the high degree of conservation of the phosphorylation sites for protein kinase C between human and mouse abl proteins suggests an important functional role.

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30

Pendergast, A. M., J. A. Traugh, and O. N. Witte. "Normal cellular and transformation-associated abl proteins share common sites for protein kinase C phosphorylation." Molecular and Cellular Biology 7, no. 12 (December 1987): 4280–89. http://dx.doi.org/10.1128/mcb.7.12.4280-4289.1987.

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Viral transduction and chromosomal translocations of the c-abl gene result in the synthesis of abl proteins with structurally altered amino termini. These altered forms of the abl protein, but not the c-abl proteins, are detectably phosphorylated on tyrosine in vivo. In contrast, all forms of the abl protein are phosphorylated on serine following in vivo labeling with Pi. Treatment of NIH-3T3 cells with protein kinase C activators resulted in a four- to eightfold increase in the phosphorylation of murine c-abl due to modification of two serines on the c-abl protein. Purified protein kinase C phosphorylated all abl proteins at the same two sites. Both sites are precisely conserved in murine and human abl proteins. The sites on the abl proteins were found near the carboxy terminus. In contrast, for the epidermal growth factor receptor (T. Hunter, N. Ling, and J. A. Cooper, Nature [London] 311:480-483, 1984) and pp60src (K. L. Gould, J. R. Woodgett, J. A. Cooper, J. E. Buss, D. Shalloway, and T. Hunter, Cell 42:849-857, 1985), the sites of protein kinase C phosphorylation are amino-terminal to the kinase domain. The abl carboxy-terminal region is not necessary for the tyrosine kinase activity or transformation potential of the viral abl protein and may represent a regulatory domain. Using an in vitro immune complex kinase assay, we were not able to correlate reproducible changes in c-abl activity with phosphorylation by protein kinase C. However, the high degree of conservation of the phosphorylation sites for protein kinase C between human and mouse abl proteins suggests an important functional role.

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31

Hirai, M., and N. Shimizu. "Purification of two distinct proteins of approximate Mr 80,000 from human epithelial cells and identification as proper substrates for protein kinase C." Biochemical Journal 270, no. 3 (September 15, 1990): 583–89. http://dx.doi.org/10.1042/bj2700583.

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A Mr-80,000 acidic phosphoprotein (‘80K protein’) is a specific substrate for protein kinase C. We attempted to purify the 80K protein from a human squamous-cell carcinoma cell line, Ca9-22, by the sequential use of heat treatment, (NH4)2SO4 precipitation, Mono Q column chromatography, proRPC column chromatography and gel filtration. The 80K protein was assayed by phosphorylation in vitro by using partially purified human type III protein kinase C, and was fractionated into two distinct molecular species with slightly different Mr values, designated 80K-L and 80K-H proteins. Phosphorylation occurred mainly at serine residues of these proteins. Two-dimensional phosphopeptide maps after trypsin digestion and kinetic profiles of phosphorylation were different from each other. Ca2(+)- and phospholipid-dependency of the phosphorylation in vitro confirmed that both 80K-L and 80K-H proteins are true substrates for three subtypes of protein kinase C. The 80K-L protein was a preferential substrate for type III protein kinase C, and the 80K-H protein was phosphorylated more effectively by type I and type II protein kinase C. The possible roles of these two distinct 80K proteins in signal transduction are discussed.

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32

Fairbrother, Wayne J., Philippe Minard, Len Hall, Jean-Michel Betton, Dominique Missiakas, Jeannine M. Yon, and Robert J. P. Williams. "Nuclear magnetic resonance studies of isolated structural domains of yeast phosphoglycerate kinase." "Protein Engineering, Design and Selection" 3, no. 1 (1989): 5–11. http://dx.doi.org/10.1093/protein/3.1.5.

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33

Cox, S., and L. N. Johnson. "Expression of the phosphorylase kinase γ subunit catalytic domain in Escherichia coli." "Protein Engineering, Design and Selection" 5, no. 8 (1992): 811–19. http://dx.doi.org/10.1093/protein/5.8.811.

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34

Collins, Richard A., Sharon M. Kelly, Nicholas C. Price, Linda A. Fothergill-Gilmore, and Hilary Muirhead. "Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase." "Protein Engineering, Design and Selection" 9, no. 12 (1996): 1203–10. http://dx.doi.org/10.1093/protein/9.12.1203.

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35

Kau, Jyh-Hwa, and Ling-Pai Ting. "Phosphorylation of the Core Protein of Hepatitis B Virus by a 46-Kilodalton Serine Kinase." Journal of Virology 72, no. 5 (May 1, 1998): 3796–803. http://dx.doi.org/10.1128/jvi.72.5.3796-3803.1998.

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ABSTRACT Core protein is the major component of the core particle (nucleocapsid) of human hepatitis B virus. Core particles and core proteins are involved in a number of important functions in the replication cycle of the virus, including RNA packaging, DNA synthesis, and recognition of viral envelope proteins. Core protein is a phosphoprotein with most, if not all, of the phosphorylation on C-terminal serine residues. In this study, we identified a serine kinase activity from the ribosome-associated protein fraction of cytoplasm that could specifically bind and phosphorylate the C-terminal portion of recombinant core protein. This kinase is referred to as core-associated kinase (CAK). CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns. By using a far-Western assay, three specific proteins, of 46, 35, and 13 kDa, were shown to interact with the C-terminal part of the core protein. These three proteins were present only in the eluted fractions that contains the CAK activity. An in-gel kinase assay showed that a 46-kDa kinase in the same fraction could bind and phosphorylate the C-terminal part of the recombinant core protein. These results indicate that this 46-kDa kinase is most probably CAK. A similar 46-kDa kinase, which exhibits the same profile of sensitivity to kinase inhibitors as that of CAK, is present in both purified intracellular core particles and extracellular 42-nm virions, suggesting that CAK is a candidate for the core particle-associated kinase.

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36

Klinbunga, Sirawut, Sasithorn Petkorn, Narumon Phaonakrop, Sirithorn Janpoom, Sirikan Prasertlux, Puttawan Rongmung, Sittiruk Roytrakul, Piamsak Menasveta, and Bavornlak Khamnamtong. "Comparative Proteomics for Identification of ReproductionRelated Proteins in Testes of the Giant Tiger Shrimp Penaeus monodon." Genetics of Aquatic Organisms 4, no. 2 (August 19, 2020): 69–79. http://dx.doi.org/10.4194/2459-1831-v4_2_02.

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Testicular proteome of wild and domesticated 14- and 18-month-old broodstock of the giant tiger shrimp Penaeus monodon was examined. Among 344 differentially expressed proteins identified, 11 proteins (e.g. p97/VCP-binding protein p135, lipoxygenase homology domains 1 and dipeptidyl-peptidase, accounting for 4.95% of proteins with known functions) were found in wild broodstock but not in domesticated broodstock while 152 (68.47%) proteins were commonly found in all groups of samples. Reproduction-related proteins such as vasa-like protein, Wee1-like protein kinase, serine/threonine protein kinase, mitogen activated protein kinase kinase 2, GTP-binding protein alpha subunit, seven membrane helix receptor, nuclear receptor subfamily 3, were identified. To examine a possible role of the signal transduction system in development of testes of P. monodon, the expression level of testicular serine/arginine rich-protein kinase 3 (PmSrpk3) mRNA of domesticated juveniles and broodstock was examined and it was significantly lower than that of wild P. monodon broodstock (P<0.05). PmSrpk3 expression was significantly induced by serotonin (P<0.05) but not progesterone (P>0.05) injection. The expression profiles of PmSrpk3 indicated reduced reproductive maturation of domesticated male P. monodon and exogenous administration of serotonin may be applied for promoting the testicular development of captive P. monodon

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37

Shanker, G., and R. A. Pieringer. "Investigations on myelinogenesis in vitro: I. The occurrence of endogenous protein kinase and its role in the phosphorylation of myelin basic proteins in “Myelin-like membranes” isolated from cerebral cell cultures." Bioscience Reports 7, no. 2 (February 1, 1987): 151–57. http://dx.doi.org/10.1007/bf01121879.

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The presence of a protein kinase capable of phosphorylating endogenous as well as exogenously added myelin basic proteins has been demonstrated in a myelin-like membrane fraction isolated from reaggregating and surface adhering, primary cultures of cells dissociated from embryonic mouse brain. Only the large and small components of myelin basic proteins were found to be phosphorylated when myelin-like membrane fraction was incubated with [γ-32P]ATP. The protein kinase endogenous to the myelin-like membrane fraction was mainly of the cyclic AMP independent type. There was very little cyclic AMP dependent or cyclic GMP dependent protein kinase activities in this myelin-like fraction. Although the myelin basic proteins were the only endogenous proteins phosphorylated, protein kinase of the myelin-like membrane was capable of catalyzing the phosphorylation of exogenous substrates, such as histones.

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38

S. Shanthipriya, S. Shanthipriya, and Dr Victor A. Doss. "Active Site Prediction and Targeting Bipolar Disorder through Molecular Docking Techniques on Protein Kinase Epsilon." International Journal of Scientific Research 2, no. 6 (June 1, 2012): 33–35. http://dx.doi.org/10.15373/22778179/june2013/11.

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39

Jovanović-Tucović, Maja, and Ivanka Marković. "The role of adenosine monophosphate-activated protein kinase in neurodegeneration in Parkinson's disease." Medicinski podmladak 70, no. 4 (2019): 13–20. http://dx.doi.org/10.5937/mp70-23730.

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40

Yonemoto, W., M. L. McGlone, B. Grant, and S. S. Taylor. "Autophosphorylation of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli." Protein Engineering Design and Selection 10, no. 8 (August 1, 1997): 915–25. http://dx.doi.org/10.1093/protein/10.8.915.

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41

Munir, Khan M., David C. French, Dipak K. Dube, and Lawrence A. Loeb. "Herpes thymidine kinase mutants with altered catalytic efficiencies obtained by random sequence selection." "Protein Engineering, Design and Selection" 7, no. 1 (1994): 83–89. http://dx.doi.org/10.1093/protein/7.1.83.

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42

Endicott, J. A., P. Nurse, and L. N. Johnson. "Mutational analysis supports a structural model for the cell cycle protein kinase p34." "Protein Engineering, Design and Selection" 7, no. 2 (1994): 243–57. http://dx.doi.org/10.1093/protein/7.2.243.

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43

Amstutz, Patrick, Holger Koch, H. Kaspar Binz, Stefan A. Deuber, and Andreas Plückthun. "Rapid selection of specific MAP kinase-binders from designed ankyrin repeat protein libraries." Protein Engineering, Design and Selection 19, no. 5 (March 21, 2006): 219–29. http://dx.doi.org/10.1093/protein/gzl004.

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44

Ardiani, A., A. Goyke, and M. E. Black. "Mutations at serine 37 in mouse guanylate kinase confer resistance to 6-thioguanine." Protein Engineering Design and Selection 22, no. 4 (January 10, 2009): 225–32. http://dx.doi.org/10.1093/protein/gzn078.

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45

Ruan, Chun, Xinxing Ouyang, Hongzhi Liu, Song Li, Jingsi Jin, Weiyi Tang, Yu Xia, and Bing Su. "Sin1-mediated mTOR signaling in cell growth, metabolism and immune response." National Science Review 6, no. 6 (November 1, 2019): 1149–62. http://dx.doi.org/10.1093/nsr/nwz171.

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Abstract The mammalian target of rapamycin (mTOR) is an evolutionarily conserved Ser/Thr protein kinase with essential cellular function via processing various extracellular and intracellular inputs. Two distinct multi-protein mTOR complexes (mTORC), mTORC1 and mTORC2, have been identified and well characterized in eukaryotic cells from yeast to human. Sin1, which stands for Sty1/Spc1-interacting protein1, also known as mitogen-activated protein kinase (MAPK) associated protein (MAPKAP)1, is an evolutionarily conserved adaptor protein. Mammalian Sin1 interacts with many cellular proteins, but it has been widely studied as an essential component of mTORC2, and it is crucial not only for the assembly of mTORC2 but also for the regulation of its substrate specificity. In this review, we summarize our current knowledge of the structure and functions of Sin1, focusing specifically on its protein interaction network and its roles in the mTOR pathway that could account for various cellular functions of mTOR in growth, metabolism, immunity and cancer.

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46

BELLONI-OLIVI, Luisa, Madhu ANNADATA, Gary W. GOLDSTEIN, and Joseph P. BRESSLER. "Phosphorylation of membrane proteins in erythrocytes treated with lead." Biochemical Journal 315, no. 2 (April 15, 1996): 401–6. http://dx.doi.org/10.1042/bj3150401.

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In immature rat microvessels, endothelial cells and glioma cells, exposure to lead results in an increase in the level of protein kinase C in membranes. In this paper we have extended these studies to human erythrocytes and, in addition, studied the phosphorylation of membrane proteins. A significant increase in the phosphorylation of membrane cytoskeletal proteins of molecular mass 120, 80, 52 and 45 kDa was observed in human erythrocytes treated for 60 min with lead acetate at concentrations greater than 100 nM. These same proteins were phosphorylated when erythrocytes were treated for 10 min with 50 nM phorbol 12-myristate 13-acetate (PMA). Similarly, protein kinase C activity was elevated and an increase in the amount of protein kinase C-α was observed in membranes from erythrocytes exposed to concentrations of lead acetate above 100 nM. No changes, however, in the activities of cAMP-dependent protein kinase, protein phosphatases I and IIA or casein kinase were observed. Phosphorylation of these membrane proteins stimulated by lead acetate or by PMA was not observed in erythrocytes depleted of protein kinase C by a 72-h treatment with 500 nM phorbol 12,13-dibutyrate. Finally, no changes in the levels of calcium or diacylglycerol were observed in erythrocytes stimulated with 100 nM lead acetate. These results indicate that, in erythrocytes, lead acetate stimulates the phosphorylation of membrane cytoskeletal proteins by a mechanism dependent on protein kinase C. Since levels of calcium or diacylglycerols did not increase, it appears that lead may activate the enzyme by a direct interaction.

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Szyszka, R., A. Boguszewska, N. Grankowski, and J. P. Ballesta. "Differential phosphorylation of ribosomal acidic proteins from yeast cell by two endogenous protein kinases: casein kinase-2 and 60S kinase." Acta Biochimica Polonica 42, no. 3 (September 30, 1995): 357–62. http://dx.doi.org/10.18388/abp.1995_4634.

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The native 80S ribosomes isolated from Saccharomyces cerevisiae (strain W303) cells was phosphorylated by two endogenous protein kinases: multifunctional casein kinase-2 (CK-2) and specific 60S kinase. Three acidic proteins within the 60S ribosomal subunit: YP1 beta, YP1 beta' and YP2 alpha are phosphorylated by both kinases. The other two proteins: YP1 alpha and YP2 beta are predominantly phosphorylated by CK-2 but not by 60S kinase. This was confirmed in the experiment with the recombinant protein, YP2 beta, as a substrate, which is practically not phosphorylated by specific 60S kinase. These results together with the previous data based on the target amino-acid sequences suggest that, in addition to the multifunctional casein kinase-2 and specific 60S kinase, there exist probably other protein kinase(s) which phosphorylate the ribosomal acidic proteins in the cell.

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Jurcik, Jan, Barbara Sivakova, Ingrid Cipakova, Tomas Selicky, Erika Stupenova, Matus Jurcik, Michaela Osadska, Peter Barath, and Lubos Cipak. "Phosphoproteomics Meets Chemical Genetics: Approaches for Global Mapping and Deciphering the Phosphoproteome." International Journal of Molecular Sciences 21, no. 20 (October 15, 2020): 7637. http://dx.doi.org/10.3390/ijms21207637.

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Protein kinases are important enzymes involved in the regulation of various cellular processes. To function properly, each protein kinase phosphorylates only a limited number of proteins among the thousands present in the cell. This provides a rapid and dynamic regulatory mechanism that controls biological functions of the proteins. Despite the importance of protein kinases, most of their substrates remain unknown. Recently, the advances in the fields of protein engineering, chemical genetics, and mass spectrometry have boosted studies on identification of bona fide substrates of protein kinases. Among the various methods in protein kinase specific substrate identification, genetically engineered protein kinases and quantitative phosphoproteomics have become promising tools. Herein, we review the current advances in the field of chemical genetics in analog-sensitive protein kinase mutants and highlight selected strategies for identifying protein kinase substrates and studying the dynamic nature of protein phosphorylation.

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Meister, Melanie, Ana Tomasovic, Antje Banning, and Ritva Tikkanen. "Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount." International Journal of Molecular Sciences 14, no. 3 (March 1, 2013): 4854–84. http://dx.doi.org/10.3390/ijms14034854.

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Madapallimattam, G., and A. Bennick. "Phosphorylation of Salivary Proteins by Salivary Gland Protein Kinase." Journal of Dental Research 65, no. 3 (March 1986): 405–11. http://dx.doi.org/10.1177/00220345860650030601.

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