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Thematische Bibliographien / Phosphorylation / Zeitschriftenartikel

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Zeitschriftenartikel zum Thema „Phosphorylation“

Autor: Grafiati

Veröffentlicht am 4. Juni 2021

Zuletzt aktualisiert am 25. Juli 2025

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1

Hizli, Asli A., Yong Chi, Jherek Swanger, et al. "Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A–Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase." Molecular and Cellular Biology 33, no. 3 (2012): 596–604. http://dx.doi.org/10.1128/mcb.01270-12.

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ABSTRACTProtein synthesis is highly regulated via both initiation and elongation. One mechanism that inhibits elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2 kinase (eEF2K). T56 phosphorylation inactivates eEF2 and is the only known normal eEF2 functional modification. In contrast, eEF2K undergoes extensive regulatory phosphorylations that allow diverse pathways to impact elongation. We describe a new mode of eEF2 regulation and show that its phosphorylation by cyclin A–cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), dir

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Coulonval, Katia, Hugues Kooken, and Pierre P. Roger. "Coupling of T161 and T14 phosphorylations protects cyclin B–CDK1 from premature activation." Molecular Biology of the Cell 22, no. 21 (2011): 3971–85. http://dx.doi.org/10.1091/mbc.e11-02-0136.

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Mitosis is triggered by the abrupt dephosphorylation of inhibitory Y15 and T14 residues of cyclin B1–bound cyclin-dependent kinase (CDK)1 that is also phosphorylated at T161 in its activation loop. The sequence of events leading to the accumulation of fully phosphorylated cyclin B1–CDK1 complexes remains unclear. Two-dimensional gel electrophoresis allowed us to determine whether T14, Y15, and T161 phosphorylations occur on same CDK1 molecules and to characterize the physiological occurrence of their seven phosphorylation combinations. Intriguingly, in cyclin B1–CDK1, the activating T161 phosp

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ADAMS, Ryan A., Xinran LIU, David S. WILLIAMS, and Alexandra C. NEWTON. "Differential spatial and temporal phosphorylation of the visual receptor, rhodopsin, at two primary phosphorylation sites in mice exposed to light." Biochemical Journal 374, no. 2 (2003): 537–43. http://dx.doi.org/10.1042/bj20030408.

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Phosphorylation of rhodopsin critically controls the visual transduction cascade by uncoupling it from the G-protein transducin. The kinase primarily responsible for this phosphorylation is rhodopsin kinase, a substrate-regulated kinase that phosphorylates light-activated rhodopsin. Protein kinase C has been implicated in controlling the phosphorylation of both light-activated and dark-adapted rhodopsin. Two of the major rhodopsin phosphorylation sites in vivo, Ser334 and Ser338, are effective protein kinase C phosphorylation sites in vitro, while the latter is preferentially phosphorylated by

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Vanoosthuyse, Vincent, and Kevin G. Hardwick. "The Complexity of Bub1 Regulation: Phosphorylation, Phosphorylation, Phosphorylation." Cell Cycle 2, no. 2 (2003): 118–19. http://dx.doi.org/10.4161/cc.2.2.343.

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Sluzala, Zachary B., Yang Shan, Lynda Elghazi, et al. "Novel mTORC2/HSPB4 Interaction: Role and Regulation of HSPB4 T148 Phosphorylation." Cells 13, no. 23 (2024): 2000. https://doi.org/10.3390/cells13232000.

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HSPB4 and HSPB5 (α-crystallins) have shown increasing promise as neuroprotective agents, demonstrating several anti-apoptotic and protective roles in disorders such as multiple sclerosis and diabetic retinopathy. HSPs are highly regulated by post-translational modification, including deamidation, glycosylation, and phosphorylation. Among them, T148 phosphorylation has been shown to regulate the structural and functional characteristics of HSPB4 and underlie, in part, its neuroprotective capacity. We recently demonstrated that this phosphorylation is reduced in retinal tissues from patients wit

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Pant, Harish C., and Veeranna. "Neurofilament phosphorylation." Biochemistry and Cell Biology 73, no. 9-10 (1995): 575–92. http://dx.doi.org/10.1139/o95-063.

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Neurofilament proteins (NFPs) are highly phosphorylated molecules in the axonal compartment of the adult nervous system. The phosphorylation of NFP is considered an important determinant of filament caliber, plasticity, and stability. This process reflects the function of NFs during the lifetime of a neuron from differentiation in the embryo through long-term activity in the adult until aging and environmental insult leads to pathology and ultimately death. NF function is modulated by phosphorylation–dephosphorylation in each of these diverse neuronal states. In this review, we have summarized

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.511.

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Abstract We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.bloodjournal702511.

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We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (P less th

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Bhattacharyya, Sumit, Alip Borthakur, Arivarasu N. Anbazhagan, Shivani Katyal, Pradeep K. Dudeja та Joanne K. Tobacman. "Specific effects of BCL10 Serine mutations on phosphorylations in canonical and noncanonical pathways of NF-κB activation following carrageenan". American Journal of Physiology-Gastrointestinal and Liver Physiology 301, № 3 (2011): G475—G486. http://dx.doi.org/10.1152/ajpgi.00071.2011.

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To determine the impact of B cell leukemia/lymphoma (BCL) 10 on the phosphorylation of crucial mediators in NF-κB-mediated inflammatory pathways, human colonic epithelial cells were exposed to carrageenan (CGN), a sulfated polysaccharide commonly used as a food additive and known to induce NF-κB nuclear translocation by both canonical and noncanonical pathways. Phosphorylations of intermediates in inflammatory cascades, including NF-κB-inducing kinase (NIK) at Thr559, transforming growth factor-β-activating kinase (TAK) 1 at Thr184, Thr187, and Ser192, and inhibitory factor κBα (IκBα) at Ser32

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Langlais, Paul, Zhengping Yi, and Lawrence J. Mandarino. "The Identification of Raptor as a Substrate for p44/42 MAPK." Endocrinology 152, no. 4 (2011): 1264–73. http://dx.doi.org/10.1210/en.2010-1271.

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Abstract The adaptor protein raptor is the functional identifier for mammalian target of rapamycin (mTOR) complex 1 (mTORC1), acting to target mTOR to specific substrates for phosphorylation and regulation. Using HPLC-electrospray ionization tandem mass spectrometry, we confirmed the phosphorylation of raptor at Ser696, Thr706, Ser721, Ser722, Ser855, Ser859, Ser863, Thr865, Ser877, Ser881, Ser883, and Ser884 and identified Tyr692, Ser699, Thr700, Ser704, Ser854, Ser857, Ser882, Ser886, Ser887, and Thr889 as new, previously unidentified raptor phosphorylation sites. Treatment of cells with ins

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Violin, Jonathan D., Jin Zhang, Roger Y. Tsien, and Alexandra C. Newton. "A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C." Journal of Cell Biology 161, no. 5 (2003): 899–909. http://dx.doi.org/10.1083/jcb.200302125.

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Signals transduced by kinases depend on the extent and duration of substrate phosphorylation. We generated genetically encoded fluorescent reporters for PKC activity that reversibly respond to stimuli activating PKC. Specifically, phosphorylation of the reporter expressed in mammalian cells causes changes in fluorescence resonance energy transfer (FRET), allowing real time imaging of phosphorylation resulting from PKC activation. Targeting of the reporter to the plasma membrane, where PKC is activated, reveals oscillatory phosphorylation in HeLa cells in response to histamine. Each oscillation

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Vary, Thomas C., and Christopher J. Lynch. "Meal feeding enhances formation of eIF4F in skeletal muscle: role of increased eIF4E availability and eIF4G phosphorylation." American Journal of Physiology-Endocrinology and Metabolism 290, no. 4 (2006): E631—E642. http://dx.doi.org/10.1152/ajpendo.00460.2005.

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Feeding promotes protein accretion in skeletal muscle through a stimulation of the mRNA translation initiation phase of protein synthesis either secondarily to nutrient-induced rises in insulin or owing to direct effects of nutrients themselves. The present set of experiments establishes the effects of meal feeding on potential signal transduction pathways that may be important in accelerating mRNA translation initiation. Gastrocnemius muscle from male Sprague-Dawley rats trained to consume a meal consisting of rat chow was sampled before, during, and after the meal. Meal feeding enhanced the

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Norling, L. L., and M. Landt. "Comparison of Ca2+-dependent phosphorylation in viable dispersed brain cells with calmodulin-dependent protein kinase activity in cell-free preparations of rat brain." Biochemical Journal 232, no. 3 (1985): 629–35. http://dx.doi.org/10.1042/bj2320629.

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Using two depolarizing agents, veratrine and high concentrations of extracellular KCl, we studied depolarization-stimulated phosphorylations in 32P-labelled dispersed brain tissue in order to identify phosphoprotein substrates for Ca2+ - and calmodulin-dependent protein kinase activity at the cellular level, for comparison with findings in cell-free preparations. In intact brain cells, the only prominent depolarization-stimulated phosphorylation was a 77 kDa protein separated on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. This phosphorylation was dependent on external Ca2+, sin

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Dusi, S., M. Donini, and F. Rossi. "Tyrosine phosphorylation and activation of NADPH oxidase in human neutrophils: a possible role for MAP kinases and for a 75 kDa protein." Biochemical Journal 304, no. 1 (1994): 243–50. http://dx.doi.org/10.1042/bj3040243.

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Challenge of neutrophils with concanavalin A (ConA), formyl-methionyl-leucyl-phenylalanine (FMLP), and phorbol 12-myristate 13-acetate (PMA) induced the tyrosine phosphorylation of several proteins. Among these proteins we have identified two mitogen-activated protein kinase (MAPK) isoforms of 43 kDa (p43 MAPK) and 45 kDa (p45 MAPK) molecular mass. Moreover here we show that: (1) FMLP induced the tyrosine phosphorylation of the p43 MAPK, and ConA that of p45 MAPK, while PMA induced the tyrosine phosphorylation of both p43 and p45 MAPK; all these agonists induced the tyrosine phosphorylation of

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Kabachnik, M. I., L. S. Zakharov, E. I. Goryunov, and I. Yu Kudryavtsev. "Catalytic phosphorylation of polyfluoroalkanols. 11. ?-Polyfluoroalkylbenzyldichlorophosphates as phosphorylating agents in the catalytic phosphorylation of primary polyfluoroalkanols." Bulletin of the Academy of Sciences of the USSR Division of Chemical Science 38, no. 7 (1989): 1522–26. http://dx.doi.org/10.1007/bf00978451.

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KNEBEL, Axel, Claire E. HAYDON, Nick MORRICE, and Philip COHEN. "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and −insensitive pathways." Biochemical Journal 367, no. 2 (2002): 525–32. http://dx.doi.org/10.1042/bj20020916.

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Eukaryotic elongation factor 2 (eEF2) kinase, the enzyme that inactivates eEF2, is controlled by phosphorylation. Previous work showed that stress-activated protein kinase 4 (SAPK4, also called p38Δ) inhibits eEF2 kinase in vitro by phosphorylating Ser-359, while ribosomal protein S6 kinases inhibit eEF2 kinase by phosphorylating Ser-366 [Knebel, Morrice and Cohen (2001) EMBO J. 20, 4360—4369; Wang, Li, Williams, Terada, Alessi and Proud (2001) EMBO J. 20, 4370—4379]. In the present study we have examined the effects of the protein synthesis inhibitor anisomycin and tumour necrosis factor-α (T

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Harper, Mary-Ellen, and Martin D. Brand. "Hyperthyroidism stimulates mitochondrial proton leak and ATP turnover in rat hepatocytes but does not change the overall kinetics of substrate oxidation reactions." Canadian Journal of Physiology and Pharmacology 72, no. 8 (1994): 899–908. http://dx.doi.org/10.1139/y94-127.

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Thyroid hormones have well-known effects on oxidative phosphorylation, but there is little quantitative information on their important sites of action. We have used top-down elasticity analysis, an extension of metabolic control analysis, to identify the sites of action of thyroid hormones on oxidative phosphorylation in rat hepatocytes. We divided the oxidative phosphorylation system into three blocks of reactions: the substrate oxidation subsystem, the phosphorylating subsystem, and the mitochondrial proton leak subsystem and have identified those blocks of reactions whose kinetics are signi

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Cohen, M. E., G. W. Sharp, and M. Donowitz. "Suggestion of a role for calmodulin and phosphorylation in regulation of rabbit ileal electrolyte transport: effects of promethazine." American Journal of Physiology-Gastrointestinal and Liver Physiology 251, no. 5 (1986): G710—G717. http://dx.doi.org/10.1152/ajpgi.1986.251.5.g710.

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Suggestion of a role for protein phosphorylation in the regulation of intestinal active NaCl transport was found by studying the effects of low concentrations of promethazine on Ca2+-calmodulin (CaM)-dependent protein phosphorylation of ileal microvillus membranes and on active ileal electrolyte transport. Ca2+-CaM increased the phosphorylation of six microvillus peptides (Mr 137,000, 116,000, 77,000, 58,000, 53,000, and 50,000) in a concentration-dependent manner. Promethazine inhibited the Ca2+-CaM-induced increases in each of these phosphorylations. The effect of promethazine was concentrat

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Scheid, Michael P., Paola A. Marignani, and James R. Woodgett. "Multiple Phosphoinositide 3-Kinase-Dependent Steps in Activation of Protein Kinase B." Molecular and Cellular Biology 22, no. 17 (2002): 6247–60. http://dx.doi.org/10.1128/mcb.22.17.6247-6260.2002.

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ABSTRACT The protein kinase B (PKB)/Akt family of serine kinases is rapidly activated following agonist-induced stimulation of phosphoinositide 3-kinase (PI3K). To probe the molecular events important for the activation process, we employed two distinct models of posttranslational inducible activation and membrane recruitment. PKB induction requires phosphorylation of two critical residues, threonine 308 in the activation loop and serine 473 near the carboxyl terminus. Membrane localization of PKB was found to be a primary determinant of serine 473 phosphorylation. PI3K activity was equally im

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Benes, Cyril, та Stephen P. Soltoff. "Modulation of PKCδ tyrosine phosphorylation and activity in salivary and PC-12 cells by Src kinases". American Journal of Physiology-Cell Physiology 280, № 6 (2001): C1498—C1510. http://dx.doi.org/10.1152/ajpcell.2001.280.6.c1498.

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Protein kinase C (PKC) δ becomes tyrosine phosphorylated in rat parotid acinar cells exposed to muscarinic and substance P receptor agonists, which initiate fluid secretion in this salivary cell. Here we examine the signaling components of PKCδ tyrosine phosphorylation and effects of phosphorylation on PKCδ activity. Carbachol- and substance P-promoted increases in PKCδ tyrosine phosphorylation were blocked by inhibiting phospholipase C (PLC) but not by blocking intracellular Ca2+ concentration elevation, suggesting that diacylglycerol, rather than d- myo-inositol 1,4,5-trisphosphate productio

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Solomon, M. J., T. Lee, and M. W. Kirschner. "Role of phosphorylation in p34cdc2 activation: identification of an activating kinase." Molecular Biology of the Cell 3, no. 1 (1992): 13–27. http://dx.doi.org/10.1091/mbc.3.1.13.

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Phosphorylation of p34cdc2 can both positively and negatively regulate its kinase activity. We have mapped two phosphorylation sites in Xenopus p34cdc2 to Thr-14 and Tyr-15 within the putative ATP-binding region of p34cdc2. Mutation of these sites to Ala-14 and Phe-15 has no effect on the final histone H1 kinase activity of the cyclin/p34cdc2 complex. Phosphopeptide analysis shows that there is at least one more site of phosphorylation on p34cdc2. When Thr-161 is changed to Ala, two phosphopeptide spots disappear and it is no longer possible to activate the H1 kinase activity of p34cdc2. We su

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Vendelbo, M. H., A. B. Møller, J. T. Treebak, et al. "Sustained AS160 and TBC1D1 phosphorylations in human skeletal muscle 30 min after a single bout of exercise." Journal of Applied Physiology 117, no. 3 (2014): 289–96. http://dx.doi.org/10.1152/japplphysiol.00044.2014.

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Background: phosphorylation of AS160 and TBC1D1 plays an important role for GLUT4 mobilization to the cell surface. The phosphorylation of AS160 and TBC1D1 in humans in response to acute exercise is not fully characterized. Objective: to study AS160 and TBC1D1 phosphorylation in human skeletal muscle after aerobic exercise followed by a hyperinsulinemic euglycemic clamp. Design: eight healthy men were studied on two occasions: 1) in the resting state and 2) in the hours after a 1-h bout of ergometer cycling. A hyperinsulinemic euglycemic clamp was initiated 240 min after exercise and in a time

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Geraghty, Kathryn M., Shuai Chen, Jean E. Harthill, et al. "Regulation of multisite phosphorylation and 14-3-3 binding of AS160 in response to IGF-1, EGF, PMA and AICAR." Biochemical Journal 407, no. 2 (2007): 231–41. http://dx.doi.org/10.1042/bj20070649.

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AS160 (Akt substrate of 160 kDa) mediates insulin-stimulated GLUT4 (glucose transporter 4) translocation, but is widely expressed in insulin-insensitive tissues lacking GLUT4. Having isolated AS160 by 14-3-3-affinity chromatography, we found that binding of AS160 to 14-3-3 isoforms in HEK (human embryonic kidney)-293 cells was induced by IGF-1 (insulin-like growth factor-1), EGF (epidermal growth factor), PMA and, to a lesser extent, AICAR (5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside). AS160-14-3-3 interactions were stabilized by chemical cross-linking and abolished by dephosphorylatio

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Greiwe, Julia F., Thomas C. R. Miller, Julia Locke, et al. "Structural mechanism for the selective phosphorylation of DNA-loaded MCM double hexamers by the Dbf4-dependent kinase." Nature Structural & Molecular Biology 29, no. 1 (2021): 10–20. http://dx.doi.org/10.1038/s41594-021-00698-z.

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AbstractLoading of the eukaryotic replicative helicase onto replication origins involves two MCM hexamers forming a double hexamer (DH) around duplex DNA. During S phase, helicase activation requires MCM phosphorylation by Dbf4-dependent kinase (DDK), comprising Cdc7 and Dbf4. DDK selectively phosphorylates loaded DHs, but how such fidelity is achieved is unknown. Here, we determine the cryogenic electron microscopy structure of Saccharomyces cerevisiae DDK in the act of phosphorylating a DH. DDK docks onto one MCM ring and phosphorylates the opposed ring. Truncation of the Dbf4 docking domain

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Almagor, Lior, Ivan S. Ufimtsev, Aruna Ayer, Jingzhi Li, and William I. Weis. "Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2." Proceedings of the National Academy of Sciences 116, no. 22 (2019): 10804–12. http://dx.doi.org/10.1073/pnas.1821514116.

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Metazoan cell polarity is controlled by a set of highly conserved proteins. Lethal giant larvae (Lgl) functions in apical-basal polarity through phosphorylation-dependent interactions with several other proteins as well as the plasma membrane. Phosphorylation of Lgl by atypical protein kinase C (aPKC), a component of the partitioning-defective (Par) complex in epithelial cells, excludes Lgl from the apical membrane, a crucial step in the establishment of epithelial cell polarity. We present the crystal structures of human Lgl2 in both its unphosphorylated and aPKC-phosphorylated states. Lgl2 a

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Hamáková, Kateřina, David Potěšil, Ondřej Bernatik, et al. "Semiquantitative Assessment of Dishevelled-3 Phosphorylation Status by Mass Spectrometry." Hungarian Journal of Industry and Chemistry 46, no. 1 (2018): 3–6. http://dx.doi.org/10.1515/hjic-2018-0002.

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Abstract The focus of this paper is the human Dishevelled 3 protein (hDvl3), an essential component of the Wnt signalling pathway that contributes to their regulation. Mass spectrometry-based analysis of hDvl3 phosphorylations induced by eight associated kinases was performed revealing several dozens of phosphorylation sites. The main outcome of this study was the description of Dvl phosphorylation “patterns” induced by individual kinases

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Her, J. H., S. Lakhani, K. Zu, et al. "Dual phosphorylation and autophosphorylation in mitogen-activated protein (MAP) kinase activation." Biochemical Journal 296, no. 1 (1993): 25–31. http://dx.doi.org/10.1042/bj2960025.

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p42mapk [mitogen activated protein (MAP) kinase; extracellular signal-regulated protein kinase (ERK)] is a serine/threonine-specific protein kinase that is activated by dual tyrosine and threonine phosphorylation in response to diverse agonists. Both the tyrosine and threonine phosphorylations are necessary for full enzymic activity. A MAP kinase activator recently purified and cloned has been shown to be a protein kinase (MAP kinase kinase) that is able to induce the dual phosphorylation of MAP kinase on both the regulatory tyrosine and threonine sites in vitro. In the present paper we have u

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Maik-Rachline, Galia, Shmuel Shaltiel, and Rony Seger. "Extracellular phosphorylation converts pigment epithelium–derived factor from a neurotrophic to an antiangiogenic factor." Blood 105, no. 2 (2005): 670–78. http://dx.doi.org/10.1182/blood-2004-04-1569.

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Abstract The pigment epithelium–derived factor (PEDF) belongs to the superfamily of serine protease inhibitors (serpin). There have been 2 distinct functions attributed to this factor, which can act either as a neurotrophic or as an antiangiogenic factor. Besides its localization in the eye, PEDF was recently reported to be present also in human plasma. We found that PEDF purified from plasma is a phosphoprotein, which is extracellularly phosphorylated by protein kinase CK2 (CK2) and to a lesser degree, intracellularly, by protein kinase A (PKA). CK2 phosphorylates PEDF on 2 main residues, Ser

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Amano, Mutsuki, Yoko Kanazawa, Kei Kozawa, and Kozo Kaibuchi. "Identification of the Kinase-Substrate Recognition Interface between MYPT1 and Rho-Kinase." Biomolecules 12, no. 2 (2022): 159. http://dx.doi.org/10.3390/biom12020159.

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Protein kinases exert physiological functions through phosphorylating their specific substrates; however, the mode of kinase–substrate recognition is not fully understood. Rho-kinase is a Ser/Thr protein kinase that regulates cytoskeletal reorganization through phosphorylating myosin light chain (MLC) and the myosin phosphatase targeting subunit 1 (MYPT1) of MLC phosphatase (MLCP) and is involved in various diseases, due to its aberrant cellular contraction, morphology, and movement. Despite the importance of the prediction and identification of substrates and phosphorylation sites, understand

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Zheng, Yupeng, Sam John, James J. Pesavento, et al. "Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II." Journal of Cell Biology 189, no. 3 (2010): 407–15. http://dx.doi.org/10.1083/jcb.201001148.

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Histone H1 phosphorylation affects chromatin condensation and function, but little is known about how specific phosphorylations impact the function of H1 variants in higher eukaryotes. In this study, we show that specific sites in H1.2 and H1.4 of human cells are phosphorylated only during mitosis or during both mitosis and interphase. Antisera generated to individual H1.2/H1.4 interphase phosphorylations reveal that they are distributed throughout nuclei and enriched in nucleoli. Moreover, interphase phosphorylated H1.4 is enriched at active 45S preribosomal RNA gene promoters and is rapidly

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Thornton, Tina, та Mercedes Rincon. "The role of p38 MAPK/GSK3β signaling in T and B lymphocytes undergoing programmed DNA recombination (111.47)". Journal of Immunology 188, № 1_Supplement (2012): 111.47. http://dx.doi.org/10.4049/jimmunol.188.supp.111.47.

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Abstract In addition to environmentally induced DNA double strand breaks (DSBs), developmentally programmed DSBs are also generated in T and B cells during V(D)J recombination. We have shown that in response to DSBs, p38 MAPK is activated and translocated to the nucleus. Although typically associated with cell death, we found that p38 MAPK promoted survival of cells following DNA damage by phosphorylating GSK3β at a novel residue (S389). GSK3β is a constitutively active kinase that can promote death by phosphorylating and targeting survival factors for destruction. GSK3β has been shown to be i

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Soltys, Carrie-Lynn M., Suzanne Kovacic, and Jason R. B. Dyck. "Activation of cardiac AMP-activated protein kinase by LKB1 expression or chemical hypoxia is blunted by increased Akt activity." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 6 (2006): H2472—H2479. http://dx.doi.org/10.1152/ajpheart.01206.2005.

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AMP-activated protein kinase (AMPK) plays a major role in the regulation of cardiac energy substrate utilization and can be negatively regulated by Akt activation in the heart. It has recently been shown that Akt directly phosphorylates AMPKα1/α2 on Ser485/491 in vitro and prevents the AMPK kinase (AMPKK) LKB1 from phosphorylating AMPKα at its primary activation site, Thr172 (S Horman, D Vertommen, R Heath, D Neumann, V Mouton, A Woods, U Schlattner, T Wallimann, D Carling, L Hue, and MH Rider. J Biol Chem 281: 5335–5340, 2006). To determine whether this is also the case in the cardiac myocyte

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Akiyama, T., T. Saito, H. Ogawara, K. Toyoshima, and T. Yamamoto. "Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells." Molecular and Cellular Biology 8, no. 3 (1988): 1019–26. http://dx.doi.org/10.1128/mcb.8.3.1019-1026.1988.

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Treatment of human adenocarcinoma MKN-7 cells with epidermal growth factor (EGF) or phorbol tetradecanoate acetate (TPA) stimulated phosphorylation of the c-erbB-2 gene product. EGF induced a rapid increase in phosphotyrosine followed by relatively gradual increases in phosphoserine and phosphothreonine. On the other hand, the TPA-induced increase in phosphorylations occurred exclusively on serine and threonine residues. Tryptic phosphopeptide mapping analysis suggested that treatments with EGF and TPA induced phosphorylation of many common sites in the c-erbB-2 gene product. However, in contr

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Akiyama, T., T. Saito, H. Ogawara, K. Toyoshima, and T. Yamamoto. "Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells." Molecular and Cellular Biology 8, no. 3 (1988): 1019–26. http://dx.doi.org/10.1128/mcb.8.3.1019.

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Treatment of human adenocarcinoma MKN-7 cells with epidermal growth factor (EGF) or phorbol tetradecanoate acetate (TPA) stimulated phosphorylation of the c-erbB-2 gene product. EGF induced a rapid increase in phosphotyrosine followed by relatively gradual increases in phosphoserine and phosphothreonine. On the other hand, the TPA-induced increase in phosphorylations occurred exclusively on serine and threonine residues. Tryptic phosphopeptide mapping analysis suggested that treatments with EGF and TPA induced phosphorylation of many common sites in the c-erbB-2 gene product. However, in contr

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Ahn, Jae Suk, Andrea Musacchio, Marina Mapelli, et al. "Development of an Assay to Screen for Inhibitors of Tau Phosphorylation by Cdk5." Journal of Biomolecular Screening 9, no. 2 (2004): 122–31. http://dx.doi.org/10.1177/1087057103260594.

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A high-throughput assay for tau phosphorylation by cdk5/p25 is described. Full-length recombinant tau was used as a substrate in the presence of saturating adenosine triphosphate (ATP). Using PHF-1, an antibody directed specifically against 2 tau phosphorylation epitopes (serine 396 and serine 404), an enzyme-linked immunosorbent assay (ELISA)- based colorimetric assay was formatted in 384-well plates. The assay was validated by measuring kinetic parameters for cdk5/p25 catalysis and known inhibitors. Rate constants for the site-specific phosphorylations at the PHF-1 epitopes were determined a

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Vilimek, Dino, and Vincent Duronio. "Cytokine-stimulated phosphorylation of GSK-3 is primarily dependent upon PKCs, not PKB." Biochemistry and Cell Biology 84, no. 1 (2006): 20–29. http://dx.doi.org/10.1139/o05-154.

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The regulation of glycogen synthase kinase-3 (GSK-3) by phosphorylation at inhibitory sites has been well documented. In many, but not all, cases, the phosphatidylinositol 3-kinase pathway, and particularly the downstream kinase protein kinase B (PKB) / akt, have been shown to be responsible for GSK-3 phosphorylation. Given that no studies have ever reported cytokine-mediated phosphorylation of GSK-3, we investigated the phosphorylation of this kinase in several hemopoietic cell types in response to either interleukin (IL)-3, IL-4 or granulocyte-macrophage colony stimulating factor (GM-CSF). E

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Ogura, Masato, Junko Yamaki, Miwako K. Homma, and Yoshimi Homma. "Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components." Biochemical Journal 447, no. 2 (2012): 281–89. http://dx.doi.org/10.1042/bj20120509.

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Mitochondrial protein tyrosine phosphorylation is an important mechanism for the modulation of mitochondrial functions. In the present study, we have identified novel substrates of c-Src in mitochondria and investigated their function in the regulation of oxidative phosphorylation. The Src family kinase inhibitor PP2 {amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4d] pyrimidine} exhibits significant reduction of respiration. Similar results were obtained from cells expressing kinase-dead c-Src, which harbours a mitochondrial-targeting sequence. Phosphorylation-site analysis selects c-Src ta

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Matusiak, Magdalena, Nina Van Opdenbosch, Lieselotte Vande Walle, Jean-Claude Sirard, Thirumala-Devi Kanneganti, and Mohamed Lamkanfi. "Flagellin-induced NLRC4 phosphorylation primes the inflammasome for activation by NAIP5." Proceedings of the National Academy of Sciences 112, no. 5 (2015): 1541–46. http://dx.doi.org/10.1073/pnas.1417945112.

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The Nlrc4 inflammasome contributes to immunity against intracellular pathogens that express flagellin and type III secretion systems, and activating mutations in NLRC4 cause autoinflammation in patients. Both Naip5 and phosphorylation of Nlrc4 at Ser533 are required for flagellin-induced inflammasome activation, but how these events converge upon inflammasome activation is not known. Here, we showed that Nlrc4 phosphorylation occurs independently of Naip5 detection of flagellin because Naip5 deletion in macrophages abolished caspase-1 activation, interleukin (IL)-1β secretion, and pyroptosis,

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Shimasaki, Kentaro, Keigo Kumagai, Shota Sakai, Toshiyuki Yamaji, and Kentaro Hanada. "Hyperosmotic Stress Induces Phosphorylation of CERT and Enhances Its Tethering throughout the Endoplasmic Reticulum." International Journal of Molecular Sciences 23, no. 7 (2022): 4025. http://dx.doi.org/10.3390/ijms23074025.

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The ceramide transport protein (CERT) delivers ceramide from the endoplasmic reticulum (ER) to the Golgi apparatus, where ceramide is converted to sphingomyelin (SM). The function of CERT is regulated in two distinct phosphorylation-dependent events: multiple phosphorylations in a serine-repeat motif (SRM) and phosphorylation of serine 315 residue (S315). Pharmacological inhibition of SM biosynthesis results in an increase in SRM-dephosphorylated CERT, which serves as an activated form, and an enhanced phosphorylation of S315, which augments the binding of CERT to ER-resident VAMP-associated p

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Kurihara, Kinji, Nobuo Nakanishi, Marilyn L. Moore-Hoon, and R. James Turner. "Phosphorylation of the salivary Na+-K+-2Cl− cotransporter." American Journal of Physiology-Cell Physiology 282, no. 4 (2002): C817—C823. http://dx.doi.org/10.1152/ajpcell.00352.2001.

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We studied the phosphorylation of the secretory Na+-K+-2Cl− cotransporter (NKCC1) in rat parotid acinar cells. We have previously shown that NKCC1 activity in these cells is dramatically upregulated in response to β-adrenergic stimulation and that this upregulation correlates with NKCC1 phosphorylation, possibly due to protein kinase A (PKA). We show here that when ATP is added to purified acinar basolateral membranes (BLM), NKCC1 is phosphorylated as a result of membrane-associated protein kinase activity. Additional NKCC1 phosphorylation is seen when PKA is added to BLMs, but our data indica

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Song, Weimeng, Li Hu, Zhihui Ma, Lei Yang, and Jianming Li. "Importance of Tyrosine Phosphorylation in Hormone-Regulated Plant Growth and Development." International Journal of Molecular Sciences 23, no. 12 (2022): 6603. http://dx.doi.org/10.3390/ijms23126603.

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Protein phosphorylation is the most frequent post-translational modification (PTM) that plays important regulatory roles in a wide range of biological processes. Phosphorylation mainly occurs on serine (Ser), threonine (Thr), and tyrosine (Tyr) residues, with the phosphorylated Tyr sites accounting for ~1–2% of all phosphorylated residues. Tyr phosphorylation was initially believed to be less common in plants compared to animals; however, recent investigation indicates otherwise. Although they lack typical protein Tyr kinases, plants possess many dual-specificity protein kinases that were impl

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BABY, Y., M. TSUHAKO, and N. YOZA. "ChemInform Abstract: Phosphorylation of Biomolecules with Inorganic Phosphorylating Agents." ChemInform 25, no. 25 (2010): no. http://dx.doi.org/10.1002/chin.199425285.

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Tinsley, John H., Elena E. Ustinova, Wenjuan Xu та Sarah Y. Yuan. "Src-dependent, neutrophil-mediated vascular hyperpermeability and β-catenin modification". American Journal of Physiology-Cell Physiology 283, № 6 (2002): C1745—C1751. http://dx.doi.org/10.1152/ajpcell.00230.2002.

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The hyperpermeability response of microvessels in inflammation involves complex signaling reactions and structural modifications in the endothelium. Our goal was to determine the role of Src-family kinases (Src) in neutrophil-mediated venular hyperpermeability and possible interactions between Src and endothelial barrier components. We found that inhibition of Src abolished the increases in albumin permeability caused by C5a-activated neutrophils in intact, perfused coronary venules, as well as in cultured endothelial monolayers. Activated neutrophils increased Src phosphorylation at Tyr416, w

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Lakkireddy, Dr Suresh. "MOLECULAR ADVANCEMENTS IN PROTEIN PHOSPHORYLATION METHODOLOGIES: A RAPID REVIEW." Era's Journal of Medical Research 10, no. 2 (2023): 35–38. http://dx.doi.org/10.24041/ejmr2023.33.

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Phosphorylation, the reversible addition of phosphate groups to proteins, plays a pivotal role in regulating cellular processes, including signal transduction, cell cycle progression, and metabolism. Understanding the dynamics of phosphorylation events is crucial for unraveling complex signaling networks and identifying potential therapeutic targets in various diseases. Phosphorylation immunoassays have emerged as powerful tools for the detection and quantification of phosphorylated proteins, enabling researchers to gain insights into intricate cellular signaling pathways. This review provides

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Gaplovska-Kysela, Katarina, and Andrea Sevcovicova. "Phosphorylation." Cell Cycle 12, no. 5 (2013): 716. http://dx.doi.org/10.4161/cc.23910.

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Holt, K. H., B. G. Kasson, and J. E. Pessin. "Insulin stimulation of a MEK-dependent but ERK-independent SOS protein kinase." Molecular and Cellular Biology 16, no. 2 (1996): 577–83. http://dx.doi.org/10.1128/mcb.16.2.577.

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The Ras guanylnucleotide exchange protein SOS undergoes feedback phosphorylation and dissociation from Grb2 following insulin receptor kinase activation of Ras. To determine the serine/threonine kinase(s) responsible for SOS phosphorylation in vivo, we assessed the role of mitogen-activated, extracellular-signal-regulated protein kinase kinase (MEK), extracellular-signal-regulated protein kinase (ERK), and the c-JUN protein kinase (JNK) in this phosphorylation event. Expression of a dominant-interfering MEK mutant, in which lysine 97 was replaced with arginine (MEK/K97R), resulted in an inhibi

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Bishop, R., R. Martinez, M. J. Weber, et al. "Protein phosphorylation in a tetradecanoyl phorbol acetate-nonproliferative variant of 3T3 cells." Molecular and Cellular Biology 5, no. 9 (1985): 2231–37. http://dx.doi.org/10.1128/mcb.5.9.2231-2237.1985.

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The 3T3-TNR9 cell line is a variant of Swiss 3T3 cells which does not respond mitogenically to tumor promoters, but does respond mitogenically to epidermal growth factor, fibroblast growth factor, and serum. To elucidate differences between tumor promoters and polypeptide mitogens in the pathway(s) of mitogenesis which might be responsible for the nonresponsiveness of the 3T3-TNR9 cells, we have examined in these cells the early protein phosphorylation events known to be associated with mitogenesis in the parental 3T3 cells. We find that the 3T3-TNR9 cells display levels of tetradecanoyl phorb

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Bishop, R., R. Martinez, M. J. Weber, et al. "Protein phosphorylation in a tetradecanoyl phorbol acetate-nonproliferative variant of 3T3 cells." Molecular and Cellular Biology 5, no. 9 (1985): 2231–37. http://dx.doi.org/10.1128/mcb.5.9.2231.

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The 3T3-TNR9 cell line is a variant of Swiss 3T3 cells which does not respond mitogenically to tumor promoters, but does respond mitogenically to epidermal growth factor, fibroblast growth factor, and serum. To elucidate differences between tumor promoters and polypeptide mitogens in the pathway(s) of mitogenesis which might be responsible for the nonresponsiveness of the 3T3-TNR9 cells, we have examined in these cells the early protein phosphorylation events known to be associated with mitogenesis in the parental 3T3 cells. We find that the 3T3-TNR9 cells display levels of tetradecanoyl phorb

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Drepper, Friedel, Jacek Biernat, Senthilvelrajan Kaniyappan, et al. "A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications." Journal of Biological Chemistry 295, no. 52 (2020): 18213–25. http://dx.doi.org/10.1074/jbc.ra120.015882.

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Abnormal changes of neuronal Tau protein, such as phosphorylation and aggregation, are considered hallmarks of cognitive deficits in Alzheimer's disease. Abnormal phosphorylation is thought to precede aggregation and therefore to promote aggregation, but the nature and extent of phosphorylation remain ill-defined. Tau contains ∼85 potential phosphorylation sites, which can be phosphorylated by various kinases because the unfolded structure of Tau makes them accessible. However, methodological limitations (e.g. in MS of phosphopeptides, or antibodies against phosphoepitopes) led to conflicting

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L'Allemain, G., J. H. Her, J. Wu, T. W. Sturgill, and M. J. Weber. "Growth factor-induced activation of a kinase activity which causes regulatory phosphorylation of p42/microtubule-associated protein kinase." Molecular and Cellular Biology 12, no. 5 (1992): 2222–29. http://dx.doi.org/10.1128/mcb.12.5.2222-2229.1992.

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p42/microtubule-associated protein kinase (p42mapk) is activated by tyrosine and threonine phosphorylation, and its regulatory phosphorylation is likely to be important in signalling pathways involved in growth control, secretion, and differentiation. Here we show that treatment of quiescent 3T3 cells with diverse agonists results in the appearance of an activity capable of causing the in vitro phosphorylation of p42mapk on the regulatory tyrosine and to a lesser extent on the regulatory threonine, resulting in enzymatic activation of the p42mapk. This p42mapk-activating activity is capable of

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