메뉴 건너뛰기




Volumn 1783, Issue 1, 2008, Pages 49-58

VRK3-mediated inactivation of ERK signaling in adult and embryonic rodent tissues

Author keywords

Extracellular signal regulated kinase; Mitogen activated protein kinase phosphatase; Vaccinia H1 related phosphatase; Vaccinia related kinase 3

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; VACCINIA RELATED KINASE 3;

EID: 38049016957     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.10.011     Document Type: Article
Times cited : (20)

References (46)
  • 1
    • 1542379726 scopus 로고    scopus 로고
    • Characterization of three paralogous members of the Mammalian vaccinia related kinase family
    • Nichols R.J., and Traktman P. Characterization of three paralogous members of the Mammalian vaccinia related kinase family. J. Biol. Chem. 279 (2004) 7934-7946
    • (2004) J. Biol. Chem. , vol.279 , pp. 7934-7946
    • Nichols, R.J.1    Traktman, P.2
  • 2
    • 0038356612 scopus 로고    scopus 로고
    • Expression of the VRK (vaccinia-related kinase) gene family of p53 regulators in murine hematopoietic development
    • Vega F.M., Gonzalo P., Gaspar M.L., and Lazo P.A. Expression of the VRK (vaccinia-related kinase) gene family of p53 regulators in murine hematopoietic development. FEBS Lett. 544 (2003) 176-180
    • (2003) FEBS Lett. , vol.544 , pp. 176-180
    • Vega, F.M.1    Gonzalo, P.2    Gaspar, M.L.3    Lazo, P.A.4
  • 4
    • 37549026472 scopus 로고    scopus 로고
    • T.H. Kang, D.Y. Park, Y.H. Choi, K.J. Kim, H.S. Yoon, K.T. Kim, Mitotic histone H3 phosphorylation by VRK1 in mammalian cells, Mol. Cell. Biol. (2007), doi:10.1128/MCB.00018-07.
  • 5
    • 33745450085 scopus 로고    scopus 로고
    • The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
    • Nichols R.J., Wiebe M.S., and Traktman P. The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol. Biol. Cell 17 (2006) 2451-2464
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2451-2464
    • Nichols, R.J.1    Wiebe, M.S.2    Traktman, P.3
  • 6
    • 0034721101 scopus 로고    scopus 로고
    • The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein
    • Lopez-Borges S., and Lazo P.A. The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein. Oncogene 19 (2000) 3656-3664
    • (2000) Oncogene , vol.19 , pp. 3656-3664
    • Lopez-Borges, S.1    Lazo, P.A.2
  • 7
    • 8644244682 scopus 로고    scopus 로고
    • p53 Stabilization and accumulation induced by human vaccinia-related kinase 1
    • Vega F.M., Sevilla A., and Lazo P.A. p53 Stabilization and accumulation induced by human vaccinia-related kinase 1. Mol. Cell. Biol. 24 (2004) 10366-10380
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10366-10380
    • Vega, F.M.1    Sevilla, A.2    Lazo, P.A.3
  • 8
    • 3042639759 scopus 로고    scopus 로고
    • Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK
    • Sevilla A., Santos C.R., Vega F.M., and Lazo P.A. Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK. J. Biol. Chem. 279 (2004) 27458-27465
    • (2004) J. Biol. Chem. , vol.279 , pp. 27458-27465
    • Sevilla, A.1    Santos, C.R.2    Vega, F.M.3    Lazo, P.A.4
  • 9
    • 5344259041 scopus 로고    scopus 로고
    • c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK)
    • Sevilla A., Santos C.R., Barcia R., Vega F.M., and Lazo P.A. c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK). Oncogene 23 (2004) 8950-8958
    • (2004) Oncogene , vol.23 , pp. 8950-8958
    • Sevilla, A.1    Santos, C.R.2    Barcia, R.3    Vega, F.M.4    Lazo, P.A.5
  • 10
    • 33646680749 scopus 로고    scopus 로고
    • The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines
    • Blanco S., Klimcakova L., Vega F.M., and Lazo P.A. The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines. FEBS J. 273 (2006) 2487-2504
    • (2006) FEBS J. , vol.273 , pp. 2487-2504
    • Blanco, S.1    Klimcakova, L.2    Vega, F.M.3    Lazo, P.A.4
  • 11
    • 33746615234 scopus 로고    scopus 로고
    • Negative regulation of ERK activity by VRK3-mediated activation of VHR phosphatase
    • Kang T.H., and Kim K.T. Negative regulation of ERK activity by VRK3-mediated activation of VHR phosphatase. Nat. Cell Biol. 8 (2006) 863-869
    • (2006) Nat. Cell Biol. , vol.8 , pp. 863-869
    • Kang, T.H.1    Kim, K.T.2
  • 13
    • 33748781446 scopus 로고    scopus 로고
    • Role of MAPKs in development and differentiation: lessons from knockout mice
    • Aouadi M., Binetruy B., Caron L., Le Marchand-Brustel Y., and Bost F. Role of MAPKs in development and differentiation: lessons from knockout mice. Biochimie 88 (2006) 1091-1098
    • (2006) Biochimie , vol.88 , pp. 1091-1098
    • Aouadi, M.1    Binetruy, B.2    Caron, L.3    Le Marchand-Brustel, Y.4    Bost, F.5
  • 15
    • 0036709020 scopus 로고    scopus 로고
    • Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling
    • Pouyssegur J., Volmat V., and Lenormand P. Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling. Biochem. Pharmacol. 64 (2002) 755-763
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 755-763
    • Pouyssegur, J.1    Volmat, V.2    Lenormand, P.3
  • 16
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • Bhalla U.S., Ram P.T., and Iyengar R. MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science 297 (2002) 1018-1023
    • (2002) Science , vol.297 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 17
    • 34547156710 scopus 로고    scopus 로고
    • Regulation of MAP kinases by MAP kinase phosphatases
    • Kondoh K., and Nishida E. Regulation of MAP kinases by MAP kinase phosphatases. Biochim. Biophys. Acta 1773 (2007) 1227-1237
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1227-1237
    • Kondoh, K.1    Nishida, E.2
  • 18
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A., and Zhou M.M. Structure and regulation of MAPK phosphatases. Cell. Signal. 16 (2004) 769-779
    • (2004) Cell. Signal. , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 19
    • 0038832564 scopus 로고    scopus 로고
    • Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation
    • Brondello J.M., Pouyssegur J., and McKenzie F.R. Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation. Science 286 (1999) 2514-2517
    • (1999) Science , vol.286 , pp. 2514-2517
    • Brondello, J.M.1    Pouyssegur, J.2    McKenzie, F.R.3
  • 20
    • 0038498118 scopus 로고    scopus 로고
    • ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway
    • Lin Y.W., Chuang S.M., and Yang J.L. ERK1/2 achieves sustained activation by stimulating MAPK phosphatase-1 degradation via the ubiquitin-proteasome pathway. J. Biol. Chem. 278 (2003) 21534-21541
    • (2003) J. Biol. Chem. , vol.278 , pp. 21534-21541
    • Lin, Y.W.1    Chuang, S.M.2    Yang, J.L.3
  • 21
    • 0033532067 scopus 로고    scopus 로고
    • Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway
    • Todd J.L., Tanner K.G., and Denu J.M. Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway. J. Biol. Chem. 274 (1999) 13271-13280
    • (1999) J. Biol. Chem. , vol.274 , pp. 13271-13280
    • Todd, J.L.1    Tanner, K.G.2    Denu, J.M.3
  • 23
    • 0029905354 scopus 로고    scopus 로고
    • Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1 a novel cytosolic dual-specificity phosphatase
    • Groom L.A., Sneddon A.A., Alessi D.R., Dowd S., and Keyse S.M. Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1 a novel cytosolic dual-specificity phosphatase. Embo. J. 15 (1996) 3621-3632
    • (1996) Embo. J. , vol.15 , pp. 3621-3632
    • Groom, L.A.1    Sneddon, A.A.2    Alessi, D.R.3    Dowd, S.4    Keyse, S.M.5
  • 24
    • 0029910140 scopus 로고    scopus 로고
    • The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases
    • Muda M., Theodosiou A., Rodrigues N., Boschert U., Camps M., Gillieron C., Davies K., Ashworth A., and Arkinstall S. The dual specificity phosphatases M3/6 and MKP-3 are highly selective for inactivation of distinct mitogen-activated protein kinases. J. Biol. Chem. 271 (1996) 27205-27208
    • (1996) J. Biol. Chem. , vol.271 , pp. 27205-27208
    • Muda, M.1    Theodosiou, A.2    Rodrigues, N.3    Boschert, U.4    Camps, M.5    Gillieron, C.6    Davies, K.7    Ashworth, A.8    Arkinstall, S.9
  • 26
    • 0041357161 scopus 로고    scopus 로고
    • Feedback regulation of MAPK signalling by an RNA-binding protein
    • Sugiura R., Kita A., Shimizu Y., Shuntoh H., Sio S.O., and Kuno T. Feedback regulation of MAPK signalling by an RNA-binding protein. Nature 424 (2003) 961-965
    • (2003) Nature , vol.424 , pp. 961-965
    • Sugiura, R.1    Kita, A.2    Shimizu, Y.3    Shuntoh, H.4    Sio, S.O.5    Kuno, T.6
  • 27
    • 14044260735 scopus 로고    scopus 로고
    • The transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development
    • Wilson M.J., Jeyasuria P., Parker K.L., and Koopman P. The transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development. J. Biol. Chem. 280 (2005) 5917-5923
    • (2005) J. Biol. Chem. , vol.280 , pp. 5917-5923
    • Wilson, M.J.1    Jeyasuria, P.2    Parker, K.L.3    Koopman, P.4
  • 28
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • Chang L., and Karin M. Mammalian MAP kinase signalling cascades. Nature 410 (2001) 37-40
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 29
    • 33847355217 scopus 로고    scopus 로고
    • Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate
    • Santos S.D., Verveer P.J., and Bastiaens P.I. Growth factor-induced MAPK network topology shapes Erk response determining PC-12 cell fate. Nat. Cell Biol. 9 (2007) 324-330
    • (2007) Nat. Cell Biol. , vol.9 , pp. 324-330
    • Santos, S.D.1    Verveer, P.J.2    Bastiaens, P.I.3
  • 30
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C., Cobb M.H., and Shaw P.E. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. Embo. J. 14 (1995) 951-962
    • (1995) Embo. J. , vol.14 , pp. 951-962
    • Gille, H.1    Kortenjann, M.2    Thomae, O.3    Moomaw, C.4    Slaughter, C.5    Cobb, M.H.6    Shaw, P.E.7
  • 31
    • 0032553412 scopus 로고    scopus 로고
    • Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2
    • Hodge C., Liao J., Stofega M., Guan K., Carter-Su C., and Schwartz J. Growth hormone stimulates phosphorylation and activation of elk-1 and expression of c-fos, egr-1, and junB through activation of extracellular signal-regulated kinases 1 and 2. J. Biol. Chem. 273 (1998) 31327-31336
    • (1998) J. Biol. Chem. , vol.273 , pp. 31327-31336
    • Hodge, C.1    Liao, J.2    Stofega, M.3    Guan, K.4    Carter-Su, C.5    Schwartz, J.6
  • 33
    • 0037107396 scopus 로고    scopus 로고
    • Signaling pathways and late-onset gene induction associated with renal mesangial cell hypertrophy
    • Goruppi S., Bonventre J.V., and Kyriakis J.M. Signaling pathways and late-onset gene induction associated with renal mesangial cell hypertrophy. Embo. J. 21 (2002) 5427-5436
    • (2002) Embo. J. , vol.21 , pp. 5427-5436
    • Goruppi, S.1    Bonventre, J.V.2    Kyriakis, J.M.3
  • 34
    • 33846118471 scopus 로고    scopus 로고
    • Statin attenuates high glucose-induced and angiotensin II-induced MAP kinase activity through inhibition of NAD(P)H oxidase activity in cultured mesangial cells
    • Yu H.Y., Inoguchi T., Nakayama M., Tsubouchi H., Sato N., Sonoda N., Sasaki S., Kobayashi K., and Nawata H. Statin attenuates high glucose-induced and angiotensin II-induced MAP kinase activity through inhibition of NAD(P)H oxidase activity in cultured mesangial cells. Med. Chem. 1 (2005) 461-466
    • (2005) Med. Chem. , vol.1 , pp. 461-466
    • Yu, H.Y.1    Inoguchi, T.2    Nakayama, M.3    Tsubouchi, H.4    Sato, N.5    Sonoda, N.6    Sasaki, S.7    Kobayashi, K.8    Nawata, H.9
  • 35
    • 27844442656 scopus 로고    scopus 로고
    • ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes
    • Liu S., Liang Y., Huang H., Wang L., Li Y., Li J., Li X., and Wang H. ERK-dependent signaling pathway and transcriptional factor Ets-1 regulate matrix metalloproteinase-9 production in transforming growth factor-beta1 stimulated glomerular podocytes. Cell. Physiol. Biochem. 16 (2005) 207-216
    • (2005) Cell. Physiol. Biochem. , vol.16 , pp. 207-216
    • Liu, S.1    Liang, Y.2    Huang, H.3    Wang, L.4    Li, Y.5    Li, J.6    Li, X.7    Wang, H.8
  • 36
    • 0036227535 scopus 로고    scopus 로고
    • ERK and p38 MAP kinase are required for rat renal development
    • Hida M., Omori S., and Awazu M. ERK and p38 MAP kinase are required for rat renal development. Kidney Int. 61 (2002) 1252-1262
    • (2002) Kidney Int. , vol.61 , pp. 1252-1262
    • Hida, M.1    Omori, S.2    Awazu, M.3
  • 37
    • 0030762565 scopus 로고    scopus 로고
    • Activation of extracellular signal-regulated kinase in proliferative glomerulonephritis in rats
    • Bokemeyer D., Guglielmi K.E., McGinty A., Sorokin A., Lianos E.A., and Dunn M.J. Activation of extracellular signal-regulated kinase in proliferative glomerulonephritis in rats. J. Clin. Invest. 100 (1997) 582-588
    • (1997) J. Clin. Invest. , vol.100 , pp. 582-588
    • Bokemeyer, D.1    Guglielmi, K.E.2    McGinty, A.3    Sorokin, A.4    Lianos, E.A.5    Dunn, M.J.6
  • 38
    • 33646153064 scopus 로고    scopus 로고
    • Induction of steroidogenesis in immature rat Leydig cells by interleukin-1alpha is dependent on extracellular signal-regulated kinases
    • Renlund N., Jo Y., Svechnikova I., Holst M., Stocco D.M., Soder O., and Svechnikov K. Induction of steroidogenesis in immature rat Leydig cells by interleukin-1alpha is dependent on extracellular signal-regulated kinases. J. Mol. Endocrinol. 36 (2006) 327-336
    • (2006) J. Mol. Endocrinol. , vol.36 , pp. 327-336
    • Renlund, N.1    Jo, Y.2    Svechnikova, I.3    Holst, M.4    Stocco, D.M.5    Soder, O.6    Svechnikov, K.7
  • 39
    • 17244373563 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases (ERK), 1 2 are required for luteinizing hormone (LH)-induced steroidogenesis in primary Leydig cells and control steroidogenic acute regulatory (StAR) expression
    • Martinat N., Crepieux P., Reiter E., and Guillou F. Extracellular signal-regulated kinases (ERK), 1 2 are required for luteinizing hormone (LH)-induced steroidogenesis in primary Leydig cells and control steroidogenic acute regulatory (StAR) expression. Reprod. Nutr. Dev. 45 (2005) 101-108
    • (2005) Reprod. Nutr. Dev. , vol.45 , pp. 101-108
    • Martinat, N.1    Crepieux, P.2    Reiter, E.3    Guillou, F.4
  • 41
    • 0033788484 scopus 로고    scopus 로고
    • A conserved docking motif in MAP kinases common to substrates activators and regulators
    • Tanoue T., Adachi M., Moriguchi T., and Nishida E. A conserved docking motif in MAP kinases common to substrates activators and regulators. Nat. Cell Biol. 2 (2000) 110-116
    • (2000) Nat. Cell Biol. , vol.2 , pp. 110-116
    • Tanoue, T.1    Adachi, M.2    Moriguchi, T.3    Nishida, E.4
  • 42
    • 0035254671 scopus 로고    scopus 로고
    • Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions
    • Tanoue T., Maeda R., Adachi M., and Nishida E. Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions. Embo. J. 20 (2001) 466-479
    • (2001) Embo. J. , vol.20 , pp. 466-479
    • Tanoue, T.1    Maeda, R.2    Adachi, M.3    Nishida, E.4
  • 43
    • 0035106342 scopus 로고    scopus 로고
    • Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2
    • Farooq A., Chaturvedi G., Mujtaba S., Plotnikova O., Zeng L., Dhalluin C., Ashton R., and Zhou M.M. Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2. Mol. Cell 7 (2001) 387-399
    • (2001) Mol. Cell , vol.7 , pp. 387-399
    • Farooq, A.1    Chaturvedi, G.2    Mujtaba, S.3    Plotnikova, O.4    Zeng, L.5    Dhalluin, C.6    Ashton, R.7    Zhou, M.M.8
  • 44
    • 0032910476 scopus 로고    scopus 로고
    • Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
    • Stewart A.E., Dowd S., Keyse S.M., and McDonald N.Q. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat. Struct. Biol. 6 (1999) 174-181
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 174-181
    • Stewart, A.E.1    Dowd, S.2    Keyse, S.M.3    McDonald, N.Q.4
  • 45
    • 10344258041 scopus 로고    scopus 로고
    • Targeting the mitogen-activated protein kinase cascade to treat cancer
    • Sebolt-Leopold J.S., and Herrera R. Targeting the mitogen-activated protein kinase cascade to treat cancer. Nat. Rev., Cancer 4 (2004) 937-947
    • (2004) Nat. Rev., Cancer , vol.4 , pp. 937-947
    • Sebolt-Leopold, J.S.1    Herrera, R.2
  • 46
    • 33646399160 scopus 로고    scopus 로고
    • Targeting the ERK signaling pathway in cancer therapy
    • Kohno M., and Pouyssegur J. Targeting the ERK signaling pathway in cancer therapy. Ann. Med. 38 (2006) 200-211
    • (2006) Ann. Med. , vol.38 , pp. 200-211
    • Kohno, M.1    Pouyssegur, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.