Regulation of tyrosine hydroxylase by stress-activated protein kinases
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Recombinant human tyrosine hydroxylase (hTH1) was found to be phosphorylated by mitogen and stress‐activated protein kinase 1 (MSK1) at Ser40 and by p38 regulated/activated kinase (PRAK) on Ser19. Phosphorylation by MSK1 induced an increase in Vmax and a decrease in Km for 6‐(R)‐5,6,7,8‐tetrahydrobiopterin (BH 4), while these kinetic parameters were unaffected as a result of phosphorylation by PRAK. Phosphorylation of both Ser40 and Ser19 induced a high‐affinity binding of 14‐3‐3 proteins, but only the interaction of 14‐3‐3 with Ser19 increased the hTH1 activity. The 14‐3‐3 proteins also inhibited the rate of dephosphorylation of Ser19 and Ser40 by 82 and 36%, respectively. The phosphorylation of hTH1 on Ser19 caused a threefold increase in the rate of phosphorylation of Ser40. These studies provide new insights into the possible roles of stress‐activated protein kinases in the regulation of catecholamine biosynthesis.
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Specificity and mechanism of action of some commonly used protein kinase inhibitors.
Davies, S., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/bj3510095 · Cited by 3,164 · see citing works
Self-citationSpecificity and mechanism of action of some commonly used protein kinase inhibitors
Davies, S., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510095 · Cited by 1,618 · see citing works
Self-citationInteraction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of Phosphoserine
Muslin, A. J., Tanner, J. W., Allen, P. M., & Shaw, A. S. (1996) · Cell · doi:10.1016/s0092-8674(00)81067-3 · Cited by 1,380 · see citing works
Deák, M., Clifton, A. D., Lucocq, J. M., & Alessi, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4426 · Cited by 992 · see citing works
[37] Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle
Cohen, P., Alemany, S., Therese, B. A., Resink, J., Strålfors, P., & Tung, H. Y. L. (1988) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(88)59039-0 · Cited by 411 · see citing works
Self-citationCasamayor, A., MORRICE, N. A., & Alessi, D. R. (1999) · Biochemical Journal · doi:10.1042/bj3420287 · Cited by 343 · see citing works
Self-citationPterin-Dependent Amino Acid Hydroxylases
Kappock, T. J., & Caradonna, J. P. (1996) · Chemical Reviews · doi:10.1021/cr9402034 · Cited by 325 · see citing works
PRAK, a novel protein kinase regulated by the p38 MAP kinase
New, L., Jiang, Y., Zhao, M., Liu, K., Zhu, W., Flood, L. J., Kato, Y., Parry, G. C. N., & Han, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3372 · Cited by 319 · see citing works
Ichimura, T., Isobe, T., Okuyama, T., Yamauchi, T., & Fujisawa, H. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81194-8 · Cited by 285 · see citing works
Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase.
Campbell, D. G., Hardie, D. G., & Vulliet, P. R. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67410-1 · Cited by 243 · see citing works
Yamauchi, T., Nakata, H., & Fujisawa, H. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69215-x · Cited by 234 · see citing works
Hefner, Y., BÖRSCH-HAUBOLD, A. G., Murakami, M., Wilde, J. I., Pasquet, S., Schieltz, D. M., Ghomashchi, F., Yates, J. R., Armstrong, C. G., Paterson, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003395200 · Cited by 232 · see citing works
Self-citationPhosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40.
Haycock, J. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38451-0 · Cited by 224 · see citing works
Reinhard, J. F., Smith, G. K., & Nichol, C. A. (1986) · Life Sciences · doi:10.1016/0024-3205(86)90395-4 · Cited by 201 · see citing works
Sutherland, C. D., ALTERIO, J., CAMPBELL, D. G., Bourdellès, B. L., Mallet, J. J., Haavik, J., & Cohen, P. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18297.x · Cited by 177 · see citing works
Self-citation[29] Assay and expression of mitogen-activated protein kinase, MAP kinase kinase, and Raf
Alessi, D. R., Cohen, P., Ashworth, A., Cowley, S. A., Leevers, S. J., & Marshall, C. J. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)55031-3 · Cited by 158 · see citing works
Self-citationHaycock, J. W., & Haycock, D. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67644-1 · Cited by 151 · see citing works
Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase.
Vulliet, P. R., Woodgett, J. R., & Cohen, P. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89798-8 · Cited by 150 · see citing works
Self-citationDistinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylases
Isobe, T., Ichimura, T., Sunaya, T., Okuyama, T., Takahashi, N., Kuwano, R., & Takahashi, Y. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90616-e · Cited by 109 · see citing works
Ni, H., Wang, X. S., Diener, K., & Yao, Z. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8135 · Cited by 108 · see citing works
Recombinant human tyrosine hydroxylase isozymes
Haavik, J., Bourdellès, B. L., Martı́nez, A., Flatmark, T., & Mallet, J. J. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16133.x · Cited by 106 · see citing works
Self-citationSalvatore, M. F., Waymire, J. C., & Haycock, J. W. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00593.x · Cited by 101 · see citing works
Stimulus-Coupled Interaction of Tyrosine Hydroxylase with 14-3-3 Proteins
Itagaki, C., Isobe, T., Taoka, M., Natsume, T., Nomura, N., Horigome, T., Omata, S., Ichinose, H., Nagatsu, T., Greene, L. A., et al. (1999) · Biochemistry · doi:10.1021/bi9914255 · Cited by 96 · see citing works
Vulliet, P. R., Woodgett, J. R., Ferrari, S. M., & Hardie, D. G. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80328-8 · Cited by 94 · see citing works
Almås, B., Bourdellès, B. L., Flatmark, T., Mallet, J. J., & Haavik, J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17283.x · Cited by 87 · see citing works
Self-citationLindgren, N., Goiny, M., Herrera‐Marschitz, M., Haycock, J. W., Hökfelt, T. G. M., & Fisone, G. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.01901.x · Cited by 86 · see citing works
Bevilaqua, L. R., Graham, M. E., Dunkley, P. R., von Nagy‐Felsobuki, E. I., & Dickson, P. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105280200 · Cited by 80 · see citing works
Salvatore, M. F., García‐España, A., Goldstein, M., Deutch, A. Y., & Haycock, J. W. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750225.x · Cited by 75 · see citing works
Kleppe, R., Toska, K., & Haavik, J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00318.x · Cited by 71 · see citing works
Self-citationHaycock, J. W., Lew, J., García‐España, A., Lee, K., Harada, K., Meller, E., & Goldstein, M. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71041670.x · Cited by 65 · see citing works
Lindgren, N., Xu, Q., Lindskog, M., Herrera‐Marschitz, M., Goiny, M., Haycock, J. W., Goldstein, M., Hökfelt, T., & Fisone, G. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0742470.x · Cited by 62 · see citing works
Thomas, G. M., Haavik, J., & Cohen, P. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.01180.x · Cited by 59 · see citing works
Self-citationLew, J. Y., García‐España, A., Lee, K. Y., Carr, K. D., Goldstein, M., Haycock, J. W., & Meller, E. (1999) · Molecular Pharmacology · doi:10.1124/mol.55.2.202 · Cited by 49 · see citing works
Site-directed mutagenesis of tyrosine hydroxylase. Role of serine 40 in catalysis.
Wu, J., Filer, D., Friedhoff, A. J., & Goldstein, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35673-4 · Cited by 38 · see citing works
Thermal Stability and CD Analysis of Rat Tyrosine Hydroxylase
Gahn, L. G., & Roskoski, R. J. (1995) · Biochemistry · doi:10.1021/bi00001a030 · Cited by 34 · see citing works
Martı́nez, A., Abeygunawardana, C., Haavik, J., Flatmark, T., & Mildvan, A. S. (1993) · Biochemistry · doi:10.1021/bi00076a011 · Cited by 31 · see citing works
Self-citationThórólfsson, M., Døskeland, A. P., Muga, A., & Martı́nez, A. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02745-x · Cited by 20 · see citing works
Phosphorylation of Tyrosine Hydroxylase in Isolated Mice Adrenal Glands
Toska, K., Kleppe, R., Cohen, P., & Haavik, J. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04435.x · Cited by 16 · see citing works
Self-citationDetermination of Phosphorylation Levels of Tyrosine Hydroxylase by Electrospray Mass Spectrometry
Graham, M. E., Dickson, P. W., Dunkley, P. R., & von Nagy‐Felsobuki, E. I. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4548 · Cited by 9 · see citing works
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Tyrosine hydroxylase and regulation of dopamine synthesis
Daubner, S. C., Le, T., & Wang, S. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.017 · Cited by 1,092 · see citing works
“This number is higher than the ones obtained using surface plasmon resonance (62).”
Result14-3-3 proteins in the nervous system
Berg, D., Holzmann, C., & Rieß, O. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1197 · Cited by 619 · see citing works
Reaction Mechanisms of Mononuclear Non-Heme Iron Oxygenases
Abu‐Omar, M. M., Loaiza, A., & Hontzeas, N. (2005) · Chemical Reviews · doi:10.1021/cr040653o · Cited by 594 · see citing works
Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
MacKintosh, C. (2004) · Biochemical Journal · doi:10.1042/bj20031332 · Cited by 527 · see citing works
Survey of the year 2003 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.726 · Cited by 505 · see citing works
Tyrosine hydroxylase phosphorylation: Regulation and consequences
Dunkley, P. R., Bobrovskaya, L., Graham, M. E., Von Nagy‐Felsobuki, E. I., & Dickson, P. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02797.x · Cited by 455 · see citing works
“Arsenite (Thomas et al. 1997; Toska et al. 2002b) and anisomycin (Bobrovskaya et al. 2001, 2004) dramatically increased the phosphorylation of TH at Ser19 but the effects were slow, only reaching maximum levels from 30 to 60 min.”
BackgroundResultInfluentialStructural basis of 14-3-3 protein functions
Obšil, T., & Obšilová, V. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.09.001 · Cited by 275 · see citing works
“but it has been suggested that 14-3-3 protein might protect proteolytically very sensitive phosphorylated regulatory domain of TH, and/or slowdown dephosphorylation of phosphorylated Ser-19 and Ser-40 [54,100,101].”
BackgroundGerits, N., Kostenko, S., Shiryaev, A., Johannessen, M., & Moens, U. L. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.02.022 · Cited by 183 · see citing works
Does α‐synuclein modulate dopaminergic synaptic content and tone at the synapse?
Sidhu, A., Wersinger, C., & Vernier, P. (2004) · The FASEB Journal · doi:10.1096/fj.03-1112rev · Cited by 163 · see citing works
“The 14-3-3 proteins also protect TH from dephosphorylation and increase the half-life of activated TH in neurons (103).”
Background14-3-3 proteins: a family of versatile molecular regulators
Obšilová, V., Šilhán, J., Bouřa, E., Teisinger, J., & Obšil, T. (2008) · Physiological Research · doi:10.33549/physiolres.931598 · Cited by 150 · see citing works
The 14-3-3 proteins in regulation of cellular metabolism
Kleppe, R., Martı́nez, A., Døskeland, S. O., & Haavik, J. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.08.008 · Cited by 147 · see citing works
Self-citationCould a loss of α‐synuclein function put dopaminergic neurons at risk?
Perez, R. G., & Hastings, T. G. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02423.x · Cited by 133 · see citing works
“Furthermore, 14-3-3 interacts with TH through an association with Ser19 and Ser40 (Kleppe et al. 2001; Toska et al. 2002), and the interaction of 14-3-3 with TH Ser19 is necessary for TH activation (Itagaki et al. 1999). a-Synuclein appears to have the opposite effect, binding TH that is less…”
BackgroundInfluentialViral vector-mediated overexpression of α-synuclein as a progressive model of Parkinson’s disease
Ulusoy, A., Decressac, M., Kirik, D., & Björklund, A. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)84005-1 · Cited by 130 · see citing works
Complex molecular regulation of tyrosine hydroxylase
Tekin, I., Roskoski, R., Carkaci-Salli, N., & Vrana, K. E. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1238-7 · Cited by 128 · see citing works
Lou, H., Montoya, S. E., Alerte, T. N. M., Wang, J., Wu, J., Peng, X., Hong, C.-S., Friedrich, E. E., Mader, S. A., Pedersen, C. J., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100867 · Cited by 115 · see citing works
Neuroprotective Function of 14-3-3 Proteins in Neurodegeneration
Shimada, T., Fournier, A., & Yamagata, K. (2013) · BioMed Research International · doi:10.1155/2013/564534 · Cited by 105 · see citing works
The Role of α‐Synuclein in Both Neuroprotection and Neurodegeneration
Sidhu, A., Wersinger, C., Moussa, C., & Vernier, P. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1332.016 · Cited by 110 · see citing works
Alerte, T. N. M., Akinfolarin, A. A., Friedrich, E. E., Mader, S. A., Hong, C.-S., & Perez, R. G. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.02.014 · Cited by 98 · see citing works
“Because phosphorylation of TH Ser19 potentiates Ser40 phosphorylation [4,19,21,40], leading to increased DA synthesis [34], our finding of high levels of phosphorylated TH in neurons bearing α-Syn aggregates (Fig 3A) suggests that TH activity and DA synthesis may be increased in the cells [32,33].”
BackgroundA survey of the year 2002 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2003) · Journal of Molecular Recognition · doi:10.1002/jmr.649 · Cited by 93 · see citing works
Tyrosine and tryptophan hydroxylases as therapeutic targets in human disease
Waløen, K., Kleppe, R., Martı́nez, A., & Haavik, J. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1272581 · Cited by 85 · see citing works
“Ser40 is targeted by cyclic nucleotide-activated kinases, as well as kinases downstream of MAPK1/2 such as MAPK-activated protein kinase 1 (MAPKAP-K1 or p90 Ribosomal S6 Kinase) and mitogen- and stress-activated kinase 1 (MSK1) that is also activated by p38 MAPKs [35,36].”
BackgroundSelf-citationTyrosine hydroxylase phosphorylation in vivo
Dunkley, P. R., & Dickson, P. W. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14675 · Cited by 85 · see citing works
“…TH stabilisation against proteolysis, conformational distortion of TH, hierarchical phosphorylation of Ser40 because of prior Ser19 phosphorylation, or inhibition of PP2A dephosphorylation of TH (Kleppe et al. 2001; Toska et al. 2002; Obsilova et al. 2008; Halskau et al. 2009; Daubner et al. 2011).”
BackgroundInfluentialDifferential Regulation of the Human Tyrosine Hydroxylase Isoforms via Hierarchical Phosphorylation
Lehmann, I. T., Bobrovskaya, L., Gordon, S. L., Dunkley, P. R., & Dickson, P. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512194200 · Cited by 81 · see citing works
Stress affects dopaminergic signaling pathways inDrosophila melanogaster
Neckameyer, W. S., & Weinstein, J. S. (2005) · Stress · doi:10.1080/10253890500147381 · Cited by 79 · see citing works
“This is consistent with other studies suggesting that protein kinases that are activated by stress-response pathways may regulate the activity of tyrosine hydroxylase (Thomas et al. 1997, Toska et al. 2002a,b).”
ResultShikano, S., Coblitz, B., Wu, M., & Li, M. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.05.006 · Cited by 79 · see citing works
Ishikawa, S., Taira, T., Niki, T., Takahashi-Niki, K., Maita, C., Maita, H., Ariga, H., & Iguchi‐Ariga, S. M. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019950 · Cited by 77 · see citing works
α-Synuclein and Dopamine Metabolism
Yu, S., Uéda, K., & Chan, P. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:243 · Cited by 77 · see citing works
“The 14-3-3 proteins also protect TH from dephosphorylation and increase the half-life of activated TH in neurons (79).”
14-3-3ζ Contributes to Tyrosine Hydroxylase Activity in MN9D Cells
Wang, J., Lou, H., Pedersen, C. J., Smith, A. D., & Perez, R. G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901310200 · Cited by 75 · see citing works
Kawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71 · see citing works
Bobrovskaya, L., Dunkley, P. R., & Dickson, P. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02550.x · Cited by 73 · see citing works
“(2004) 90, 857–864 subsequently confirmed by others both qualitatively and quantitatively (Toska et al. 2002).”
BackgroundResultInfluentialKobori, N., Clifton, G. L., & Dash, P. K. (2006) · Journal of Neurotrauma · doi:10.1089/neu.2006.23.1094 · Cited by 80 · see citing works
“Binding of 14-3-3 to TH enhances TH activity and dopamine synthesis (Toska et al., 2002; Yamauchi and Fujisawa, 1981).”
Activation and stabilization of human tryptophan hydroxylase 2 by phosphorylation and 14-3-3 binding
Winge, I., McKinney, J. A., Ying, M., D’Santos, C. S., Kleppe, R., Knappskog, P. M., & Haavik, J. (2008) · Biochemical Journal · doi:10.1042/bj20071033 · Cited by 68 · see citing works
Self-citationRodrigues, N. R., Macedo, G. E., Martins, I. K., Gomes, K. K., de Carvalho, N. R., Posser, T., & Franco, J. L. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.04.549 · Cited by 61 · see citing works
ADHD symptoms in neurometabolic diseases: Underlying mechanisms and clinical implications
Homaei, S. C., Halleland, H. B., Kleppe, R., Betari, N., Reif, A., & Haavik, J. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.11.012 · Cited by 56 · see citing works
“1) are major signaling pathways that target this site as well as multiple stress and mitogen signaling regulated kinases (Almas et al., 1992; Rodriguez-Pascual et al., 1999; Thomas et al., 1997; Toska et al., 2002).”
Self-citationDickson, P. W., & Briggs, G. D. (2013) · Advances in pharmacology · doi:10.1016/b978-0-12-411512-5.00002-6 · Cited by 53 · see citing works
Ma, F. Y., Grattan, D. R., Goffin, V., & Bunn, S. J. (2004) · Endocrinology · doi:10.1210/en.2004-0800 · Cited by 52 · see citing works
The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase
Zhang, S., Huang, T., Ilangovan, U., Hinck, A. P., & Fitzpatrick, P. F. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.12.015 · Cited by 52 · see citing works
Cruz‐Muros, I., Afonso‐Oramas, D., Abreu, P. M., Barroso‐Chinea, P., Rodrı́guez, M., González, M. C., & González‐Hernández, T. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.10.004 · Cited by 52 · see citing works
The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase
Obšilová, V., Nedbalkova, E., Šilhán, J., Bouřa, E., Heřman, P., Večeř, J., Šulc, M., Teisinger, J., Dyda, F., & Obšil, T. (2008) · Biochemistry · doi:10.1021/bi7019468 · Cited by 51 · see citing works
Kostenko, S. (2011) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v2.i5.73 · Cited by 50 · see citing works
Gordon, S. L., Bobrovskaya, L., Dunkley, P. R., & Dickson, P. W. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.10.001 · Cited by 49 · see citing works
“Phosphorylation of Ser19 does not directly increase TH activity in vitro [7]; however, incubation of Ser19-phosphorylated THwith 14-33 protein is able to produce a small increase in enzyme activity [8,9].”
BackgroundJohnson, M., Salvatore, M. F., Maiolo, S., & Bobrovskaya, L. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.01.002 · Cited by 47 · see citing works
Halskau, Ø., Ying, M., Baumann, A., Kleppe, R., Rodríguez‐Larrea, D., Almås, B., Haavik, J., & Martı́nez, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027706 · Cited by 43 · see citing works
Self-citationAcosta, G., Race, N. S., Herr, S., Fernandez, J., TANG, J. C. Y., Rogers, E. A., & Shi, R. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.06.004 · Cited by 43 · see citing works
“The 14-3-3 chaperone protein enhances the major kinases' function to activate TH at pSer40, thereby increasing DA synthesis (Itagaki et al., 1999; Tofaris et al., 2003; Toska et al., 2002).”
BackgroundInamdar, A. A., Chaudhuri, A., & O’Donnell, J. M. (2012) · Parkinson s Disease · doi:10.1155/2012/938528 · Cited by 35 · see citing works
Isom, D. G., Marguet, P., Oas, T. G., & Hellinga, H. W. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22932 · Cited by 34 · see citing works
Kuhn, M., Häbig, K., von Bonin, M., Ninkina, N. N., Buchman, V. L., Poths, S., & Rieß, O. (2007) · Neurogenetics · doi:10.1007/s10048-007-0079-z · Cited by 33 · see citing works
Moens, U. L., & Kostenko, S. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0149 · Cited by 32 · see citing works
Locomotor hyperactivity in 14-3-3ζ KO mice is associated with dopamine transporter dysfunction
Ramshaw, H., Xu, X., Jaehne, E., McCarthy, P., Greenberg, Z., Saleh, E., McClure, B., Woodcock, J., Kabbara, S., Wiszniak, S., et al. (2013) · Translational Psychiatry · doi:10.1038/tp.2013.99 · Cited by 28 · see citing works
Bevilaqua, L. R., Cammarota, M., Dickson, P. W., Sim, A. T. R., & Dunkley, P. R. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01792.x · Cited by 30 · see citing works
“Phosphory- lation of Ser19 produces no increase in TH activity (Haycock et al. 1998) unless 14-3-3 is present (Ichimura et al. 1987; Toska et al. 2002).”
BackgroundResultGerits, N., Belle, W. V., & Moens, U. L. (2007) · Behavioral and Brain Functions · doi:10.1186/1744-9081-3-58 · Cited by 29 · see citing works
Jacobsen, K. K., Kleppe, R., Johansson, S., Zayats, T., & Haavik, J. (2015) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.32339 · Cited by 28 · see citing works
“1A) [Banik et al., 1997; Itagaki et al., 1999; Toska et al., 2002; Winge et al., 2008; Kleppe et al., 2014].”
BackgroundSelf-citationNygaard, G., Szigetvari, P. D., Grindheim, A. K., Ruoff, P., Martı́nez, A., Haavik, J., Kleppe, R., & Flydal, M. I. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11111186 · Cited by 27 · see citing works
“S40 is the main site for TH activation, as its phosphorylation abrogates the binding of inhibitory CAs [97–100] and elevates the affinity for the pterin cofactor [101].”
BackgroundSelf-citationWang, S., Sura, G. R., Dangott, L. J., & Fitzpatrick, P. F. (2009) · Biochemistry · doi:10.1021/bi9004254 · Cited by 26 · see citing works
“this interaction is not settled, although it may be to protect the phosphorylated enzyme from phosphatases (33).”
BackgroundInfluentialRoyo, M., Fitzpatrick, P. F., & Daubner, S. C. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.11.007 · Cited by 26 · see citing works
Kim, Y., Kim, C., Son, S. M., Song, H., Hong, H., Han, S.-H., & Mook‐Jung, I. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0068-5 · Cited by 24 · see citing works
“PRAK is known to phosphorylate Heat shock protein 27 (HSP27) [17], cytosolic phospholipase A2 (cPLA2) [19], tyrosine hydroxylase [20], FOXO3a [21], FAK [22], septin8 [23] and p53 [24].”
BackgroundMa, F. Y., Grattan, D. R., Bobrovskaya, L., Dunkley, P. R., & Bunn, S. J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02492.x · Cited by 24 · see citing works
“E-mail: Stephen.Bunn@stonebow.otago.ac.nz Abbreviations used: AngII, angiotensin II; CaMPKII, Ca2+/calmodulin-dependent protein kinase II; CREB, protein, cAMP-responsive element binding protein; DMEM, Dulbecco’s Modified Eagles Medium; ERK1/2, extracellular regulated protein kinase 1/2; HBS, Hepes-buffered saline; MAP…”
BackgroundInfluentialSynthesis and evaluation of hexahydropyrrolo[3,4-d]isoxazole-4,6-diones as anti-stress agents
Badru, R., Anand, P., & Singh, B. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.11.037 · Cited by 23 · see citing works
Liu, B., & Arbogast, L. A. (2007) · Endocrinology · doi:10.1210/en.2007-1345 · Cited by 22 · see citing works
Kleppe, R., Rosati, S., Jorge‐Finnigan, A., Alvira, S., Ghorbani, S., Haavik, J., Valpuesta, J., Heck, A. J. R., & Martı́nez, A. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.035709 · Cited by 22 · see citing works
“Phosphorylation of TH on Ser19, by either PRAK or Ca(2) / calmodulin-dependent protein kinase II, has been found to increase the rate of Ser40 phosphorylation by PKA 2- to 3-fold, referred to as hierarchical phosphorylation (20, 22).”
InfluentialSelf-citationGhorbani, S., Fossbakk, A., Jorge‐Finnigan, A., Flydal, M. I., Haavik, J., & Kleppe, R. (2016) · Amino Acids · doi:10.1007/s00726-015-2157-0 · Cited by 22 · see citing works
“TH activity was measured as described (Toska et al. 2002; Yamauchi et al. 1981).”
BackgroundMethodInfluentialSelf-citationCao, G.-P., Gui, D., Fu, L., Guo, Z.-K., & Fu, W. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5382 · Cited by 22 · see citing works
“PP2A is important for the regulation of MAP kinases, including extracellular signal-regulated kinases 1/2, c-Jun N-terminal kinases and p38 (35), and also serves important roles in regulating tyrosine hydroxylase synthesis and α -synuclein expression (36).”
Impact of fatty acid-binding proteins and dopamine receptors on α-synucleinopathy
Kawahata, K., & Fukunaga, K. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.12.003 · Cited by 20 · see citing works
Ghorbani, S., Szigetvari, P. D., Haavik, J., & Kleppe, R. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14872 · Cited by 18 · see citing works
“…quantitatively how much of the observed cellular responses could be explained by the hierarchical effect of pSer19 on PKA mediated Ser40 phosphorylation reported in vitro (Bevilaqua et al. 2001; Toska et al. 2002), i.e. up to 3-fold increase in the rate of PKA phosphorylation of the same subunit.”
BackgroundInfluentialSelf-citationLiu, B., & Arbogast, L. A. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0335 · Cited by 18 · see citing works
“…does not directly affect TH activity, but it may potentiate TH phosphorylation at Ser-40 and subsequent TH activation by binding to the 14:3:3 protein or by hierarchical phosphorylation (Haycock et al. 1998, Bevilaqua et al. 2001, Toska et al. 2002, Bobrovskaya et al. 2004, Dunkley et al. 2004).”
Fukuda, T., Ishii, K., Nanmoku, T., Isobe, K., Kawakami, Y., & Takekoshi, K. (2007) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2007.01570.x · Cited by 18 · see citing works
He, D., & Dorit Ron, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706216200 · Cited by 17 · see citing works
Louša, P., Nedozrálová, H., Župa, E., Nováček, J., & Hritz, J. (2017) · Biophysical Chemistry · doi:10.1016/j.bpc.2017.01.003 · Cited by 17 · see citing works
The mitochondrial metabolic function of DJ‐1 is modulated by 14‐3‐3β
Weinert, M., Millet, A. M. C., Jonas, E. A., & Alavian, K. N. (2019) · The FASEB Journal · doi:10.1096/fj.201802754r · Cited by 17 · see citing works
Rosmaninho‐Salgado, J., Araújo, I. M., Álvaro, A. R., Duarte, E. P., & Cavadas, C. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04899.x · Cited by 16 · see citing works
“Besides its role on catecholamine release, the increase of intracellular [Ca2+] may regulates catecholamine synthesis, acting on Calmodulin-Dependent Protein Kinase II, which phosphorylates TH on Ser19 residue (Toska et al. 2002). stimulated by NO.”
BackgroundChuenkova, M. V., & PereiraPerrin, M. (2006) · Brain Research · doi:10.1016/j.brainres.2006.04.128 · Cited by 14 · see citing works
Fujikawa, T., Matsumura, S., Yamada, H., Inoue, K., & Fushiki, T. (2007) · Brain Research · doi:10.1016/j.brainres.2007.08.002 · Cited by 13 · see citing works
Gong, S., Zhang, J., Guo, Z., & Fu, W. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s161748 · Cited by 13 · see citing works
RetractedHerselman, M. F., & Bobrovskaya, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914618 · Cited by 12 · see citing works
“The activity of TH is regulated by almost every form of regulation, including phosphorylation at its serine residues (Ser) 19, 31 and 40 [1,84,85].”
BackgroundSachs, N. A., & Vaillancourt, R. R. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02119.x · Cited by 12 · see citing works
“…al. 1987), while the interaction between phosphoserine 19 and/or 40 with 14-3-3 helps diminish their rate of dephosphorylation (Kleppe et al. 2001; Toska et al. 2002), then these studies and the data presented here reveal a potential negative regulatory mechanism for TH activity, whereby…”
BackgroundInfluentialNT5DC2 affects the phosphorylation of tyrosine hydroxylase regulating its catalytic activity
Nakashima, A., Yamaguchi, H., Kondo, M., Furumura, T., Kodani, Y., Kaneko, Y. S., Kawata, M., Nagasaki, H., Nagatsu, T., & Ota, A. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02236-5 · Cited by 10 · see citing works
Genetic causes of Parkinson’s disease: extending the pathway
Rieß, O., Krüger, R., Hochstrasser, H., Soehn, A. S., Nuber, S., Franck, T., & Berg, D. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_29 · Cited by 9 · see citing works
“Indeed, 14-3-3 proteins have been shown to inhibit dephosphorylation leading to a prolonged stimulation of tyrosine hydroxylase (Toska et al., 2002), the key enzyme in dopamine synthesis.”
BackgroundSpecificity of the MAP kinase ERK2 for phosphorylation of tyrosine hydroxylase
Royo, M., Daubner, S. C., & Fitzpatrick, P. F. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.027 · Cited by 8 · see citing works
Kleppe, R., & Haavik, J. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.03.092 · Cited by 7 · see citing works
Self-citationLuke, T. M., & Hexum, T. D. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.06.010 · Cited by 7 · see citing works
Subcellular distribution of human tyrosine hydroxylase isoforms 1 and 4 in SH‐SY5Y cells
Kunzler, A., Sobrinho, P. G., Smith, T. A., Gelain, D. P., Moreira, J. C. F., Dunkley, P. R., & Dickson, P. W. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29279 · Cited by 6 · see citing works
“Phosphorylation of TH at Ser19 does not alter TH activity by itself but in concert with the binding of 14‐3‐3 protein can increase TH activity.(11,12) TH is essentially a cytosolic protein but in the brain is also found associated with membranes.”
BackgroundGDNF abates serum deprivation-induced tyrosine hydroxylase Ser19 phosphorylation and activity
Kobori, N., Moore, A. N., & Dash, P. K. (2006) · Brain Research · doi:10.1016/j.brainres.2006.02.111 · Cited by 5 · see citing works
Hamdon, S., Fernandez-Gonzalez, P., Omar, M. Y., González-Sepúlveda, M., Ortiz, J., & Gil, C. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109759 · Cited by 3 · see citing works
A Novel Prion Protein-Tyrosine Hydroxylase Interaction
Vicario, M., Zagari, A., Granata, V., Munari, F., Mammi, S., Bubacco, L., Skaper, S. D., & Negro, A. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140711092955 · Cited by 3 · see citing works
Le, V. Q., Eldani, M., Truong, M., & Wimalasena, K. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00696 · Cited by 1 · see citing works
Regulation of tyrosine hydroxylase by protein phosphatase 2A
Saraf, A. (2008) · doi:10.17077/etd.9lhm4w05 · Cited by 1 · see citing works
“Other kinases which are also able to phosphorylate Ser19 in vitro are PRAK (36) and MAPKAPK2 (35).”
InfluentialPhosphorylation-Regulated Cell Surface Expression of Membrane Proteins
Okamoto, Y., & Shikano, S. (2012) · InTech eBooks · doi:10.5772/38031
“, 2006), tyrosine hydroxylase (Toska et al., 2002), and Ndel1 (Johnson et al.”
BackgroundMolecular Bioengineering: From Protein Stability to Population Suicide
Marguet, P. (2010) · DukeSpace (Duke University)
Charakterisierung 14–3-3 homologer Gene und deren Bedeutung für die Parkinson'sche Erkrankung
Mosbacher, S., Holzmann, C., Hermann, K., Schwarz, N., Krüger, R., Ichimura, T., & Rieß, O. (2005) · Aktuelle Neurologie · doi:10.1055/s-2005-866634
Modeling the Dynamics of Dopamine Biosynthesis and its Regulation by Tyrosine Hydroxylase
Kleppe, R., Ghorbani, S., Fossbakk, A., Martı́nez, A., & Haavik, J. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-800044-1.00026-x
Self-citationMethionine Sulfoxide Reductase and Ubiquitin-dependent Degradation of Alpha-synuclein
Deng, Y. (2017) · KU ScholarWorks (The University of Kansas)
Catecholaminergic Axonal Remodeling in Motor Cortex of Mice Following Stroke
Said, A. (2020) · uO Research (University of Ottawa) · doi:10.20381/ruor-24285
Map Kinase-Activated Protein Kinase 5 (MK5)
Kotlyarov, A. (2012) · Springer eBooks · doi:10.1007/978-1-4419-0461-4_321
MAP Kinase-Activated Protein Kinase 5 (MK5)
Menon, M. B., & Kotlyarov, A. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_321-1
MAP Kinase-Activated Protein Kinase 5 (MK5)
Menon, M. B., & Kotlyarov, A. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_321
- Authors
- Toska, K., Kleppe, R., Armstrong, C. G., Morrice, N. A., Cohen, P., & Haavik, J.
- Affiliations
- University of Bergen (NO)
- University of Dundee (GB)
- Corresponding author
- Toska, Karen
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2002-11
- Volume
- 83
- Issue
- 4
- Pages
- 775-783
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1536745609
- Cited by
- 95
- References
- 39
- Citations by year
- 2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 1 · 2014: 3 · 2013: 6 · 2012: 3
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion, other-oa)
- Funders
- Kreftforeningen
- Universitetet i Bergen
- Norges Forskningsråd
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- tyrosine hydroxylase, c-Jun N-terminal kinase, MSK1, p38 MAPK, protein phosphorylation, 14-3-3 proteins, tetrahydrobiopterin, enzyme kinetics, catecholamine synthesis, enzyme regulation
- MeSH terms
- MAP-Kinase-Activated Kinase 2, Amino Acid Sequence, Binding Sites, Chromatography, High Pressure Liquid, Circular Dichroism, Enzyme Activation, Enzyme Stability, Humans, Kinetics, Phosphorylation, Protein Binding, Substrate Specificity, Temperature, Tyrosine 3-Monooxygenase, Protein Serine-Threonine Kinases, Cyclic AMP-Dependent Protein Kinases, Mitogen-Activated Protein Kinase 1, Surface Plasmon Resonance, Ribosomal Protein S6 Kinases, 90-kDa, Intracellular Signaling Peptides and Proteins, 14-3-3 Proteins
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