-
1
-
-
0030898417
-
Mitogen-activated protein kinase pathways
-
Robinson M.J., Cobb M.H. Mitogen-activated protein kinase pathways. Curr Opin Cell Biol. 9:1997;180-186.
-
(1997)
Curr Opin Cell Biol
, vol.9
, pp. 180-186
-
-
Robinson, M.J.1
Cobb, M.H.2
-
2
-
-
0030783156
-
The search for physiological substrates of the MAP and SAP kinases in mammalian cells
-
Cohen P. The search for physiological substrates of the MAP and SAP kinases in mammalian cells. Trends Cell Biol. 7:1997;353-361.
-
(1997)
Trends Cell Biol
, vol.7
, pp. 353-361
-
-
Cohen, P.1
-
3
-
-
0032910168
-
Organisation and regulation of mitogen-activated protein kinase signalling pathways
-
A comprehensive review which discusses the role of scaffold/anchoring proteins in the regulation and organisation of MAPK pathways from yeast to man
-
Garrington T.P., Johnson G.L. Organisation and regulation of mitogen-activated protein kinase signalling pathways. Curr Opin Cell Biol. 11:1999;211-218. A comprehensive review which discusses the role of scaffold/anchoring proteins in the regulation and organisation of MAPK pathways from yeast to man.
-
(1999)
Curr Opin Cell Biol
, vol.11
, pp. 211-218
-
-
Garrington, T.P.1
Johnson, G.L.2
-
4
-
-
0028872649
-
Specificity of receptor tyrosine kinase signalling: Transient versus sustained extracellular signal regulated kinase activation
-
Marshall C.J. Specificity of receptor tyrosine kinase signalling: transient versus sustained extracellular signal regulated kinase activation. Cell. 80:1995;179-185.
-
(1995)
Cell
, vol.80
, pp. 179-185
-
-
Marshall, C.J.1
-
5
-
-
0027423987
-
Amino acid similarity between CL100, a dual specificity MAP kinase phosphatase and cdc25
-
Keyse S.M., Ginsburg M. Amino acid similarity between CL100, a dual specificity MAP kinase phosphatase and cdc25. Trends Biochem Sci. 18:1993;377-378.
-
(1993)
Trends Biochem Sci
, vol.18
, pp. 377-378
-
-
Keyse, S.M.1
Ginsburg, M.2
-
6
-
-
0028955176
-
An emerging family of dual-specificity MAP kinase phosphatases
-
Keyse S.M. An emerging family of dual-specificity MAP kinase phosphatases. Biochim Biophys Acta. 1265:1995;152-160.
-
(1995)
Biochim Biophys Acta
, vol.1265
, pp. 152-160
-
-
Keyse, S.M.1
-
7
-
-
0027306121
-
The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts
-
Alessi D.R., Smythe C., Keyse S.M. The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts. Oncogene. 8:1993;2015-2020.
-
(1993)
Oncogene
, vol.8
, pp. 2015-2020
-
-
Alessi, D.R.1
Smythe, C.2
Keyse, S.M.3
-
8
-
-
0027358722
-
MKP-1(3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
-
Sun H., Charles C.H., Lau L.F., Tonks N.K. MKP-1(3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell. 75:1993;487-493.
-
(1993)
Cell
, vol.75
, pp. 487-493
-
-
Sun, H.1
Charles, C.H.2
Lau, L.F.3
Tonks, N.K.4
-
9
-
-
0028125887
-
Control of MAP kinase activation by the mitogen induced threonine/tyrosine phosphatase PAC-1
-
Ward Y., Gupta S., Jensen P., Wartmann M., Davis R.J., Kelly K. Control of MAP kinase activation by the mitogen induced threonine/tyrosine phosphatase PAC-1. Nature. 367:1994;651-654.
-
(1994)
Nature
, vol.367
, pp. 651-654
-
-
Ward, Y.1
Gupta, S.2
Jensen, P.3
Wartmann, M.4
Davis, R.J.5
Kelly, K.6
-
10
-
-
0029905354
-
Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytoplasmic dual-specificity phosphatase
-
Groom L.A., Sneddon A.A., Alessi D.R., Dowd S., Keyse S.M. Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytoplasmic 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
-
11
-
-
0029910140
-
The dual specificity phosphatases M3/6 and MKP-3 are highly selective for the inactivation of distinct mitogen-activated protein kinases
-
Muda M., Theodosiou A., Rodrigues N., Boschert U., Camps M., Gillieron C., Davies K., Ashworth A., Arkinstall S. The dual specificity phosphatases M3/6 and MKP-3 are highly selective for the 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
-
12
-
-
0032502671
-
The mitogen-activated protein-kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate-binding and enzymatic specificity
-
This paper demonstrates that the substrate specificity of dual specificity MKPs is determined by MAPK specific binding mediated by the noncatalytic domain of these proteins
-
Muda M., Theodosiou A., Gillieron C., Smith A., Chabert C., Camps M., Boschert U., Rodrigues N., Davies K., Ashworth A., Arkinstall S. The mitogen-activated protein-kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate-binding and enzymatic specificity. J Biol Chem. 273:1998;9323-9329. This paper demonstrates that the substrate specificity of dual specificity MKPs is determined by MAPK specific binding mediated by the noncatalytic domain of these proteins.
-
(1998)
J Biol Chem
, vol.273
, pp. 9323-9329
-
-
Muda, M.1
Theodosiou, A.2
Gillieron, C.3
Smith, A.4
Chabert, C.5
Camps, M.6
Boschert, U.7
Rodrigues, N.8
Davies, K.9
Ashworth, A.10
Arkinstall, S.11
-
13
-
-
0032557632
-
Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase
-
This paper demonstrates that on binding to ERK2, the MKP-3 switches to a high-activity form as monitored by hydrolysis of p-nitrophenylphosphate in vitro. Furthermore, this activation is specific to ERK2, indicating that this phenomenon may underlie the substrate specificity of this class of enzymes
-
Camps M., Nichols A., Gillieron C., Antonsson B., Muda M., Chabert C., Boschert U., Arkinstall S. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science. 280:1998;1262-1265. This paper demonstrates that on binding to ERK2, the MKP-3 switches to a high-activity form as monitored by hydrolysis of p-nitrophenylphosphate in vitro. Furthermore, this activation is specific to ERK2, indicating that this phenomenon may underlie the substrate specificity of this class of enzymes.
-
(1998)
Science
, vol.280
, pp. 1262-1265
-
-
Camps, M.1
Nichols, A.2
Gillieron, C.3
Antonsson, B.4
Muda, M.5
Chabert, C.6
Boschert, U.7
Arkinstall, S.8
-
14
-
-
0031775763
-
Isolation of the human genes encoding the Pyst1 and Pyst2 phosphatases: Characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases
-
Dowd S., Sneddon A.A., Keyse S.M. Isolation of the human genes encoding the Pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases. J Cell Sci. 111:1998;3389-3399.
-
(1998)
J Cell Sci
, vol.111
, pp. 3389-3399
-
-
Dowd, S.1
Sneddon, A.A.2
Keyse, S.M.3
-
15
-
-
0033538489
-
Molecular cloning and characterisation of a novel dual specificity phosphatase, MKP-5
-
Tanoue T., Moriguchi T., Nishida E. Molecular cloning and characterisation of a novel dual specificity phosphatase, MKP-5. J Biol Chem. 274:1999;19949-19956.
-
(1999)
J Biol Chem
, vol.274
, pp. 19949-19956
-
-
Tanoue, T.1
Moriguchi, T.2
Nishida, E.3
-
16
-
-
0032910476
-
Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation
-
The structure of the catalytic domain of the dual specificity phosphatase Pyst1/MKP-3 reveals that the active site is distorted in the absence of substrate, suggesting that it undergoes a conformational change on ERK2 binding. Site-directed mutagenesis is used to identify a catalytic aspartate that is critical only in the activated form of the enzyme
-
Stewart A.E., Dowd S., Keyse S.M., McDonald N.Q. Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and implications for regulated activation. Nat Struct Biol. 6:1999;174-181. The structure of the catalytic domain of the dual specificity phosphatase Pyst1/MKP-3 reveals that the active site is distorted in the absence of substrate, suggesting that it undergoes a conformational change on ERK2 binding. Site-directed mutagenesis is used to identify a catalytic aspartate that is critical only in the activated form of the enzyme.
-
(1999)
Nat Struct Biol
, vol.6
, pp. 174-181
-
-
Stewart, A.E.1
Dowd, S.2
Keyse, S.M.3
McDonald, N.Q.4
-
17
-
-
0029975476
-
Crystal structure of the dual-specificity protein phosphatase VHR
-
Yuvaniyama J., Denu J.M., Dixon J.E., Saper M.A. Crystal structure of the dual-specificity protein phosphatase VHR. Science. 272:1996;1328-1331.
-
(1996)
Science
, vol.272
, pp. 1328-1331
-
-
Yuvaniyama, J.1
Denu, J.M.2
Dixon, J.E.3
Saper, M.A.4
-
18
-
-
0030296632
-
Structure and function of the protein tyrosine phosphatases
-
Fauman E.B., Saper M.A. Structure and function of the protein tyrosine phosphatases. Trends Biochem Sci. 21:1996;413-417.
-
(1996)
Trends Biochem Sci
, vol.21
, pp. 413-417
-
-
Fauman, E.B.1
Saper, M.A.2
-
19
-
-
0029917244
-
Visualisation of intermediate and transition-state structures in protein tyrosine phosphatase catalysis
-
Denu J.M., Lohse D.L., Vijayalaksmi J., Saper M.A., Dixon J.E. Visualisation of intermediate and transition-state structures in protein tyrosine phosphatase catalysis. Proc Natl Acad Sci USA. 93:1996;2493-2498.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2493-2498
-
-
Denu, J.M.1
Lohse, D.L.2
Vijayalaksmi, J.3
Saper, M.A.4
Dixon, J.E.5
-
20
-
-
0029757347
-
Disruption of the erp/mkp-1 gene does not affect mouse development: Normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts
-
Dorfman K., Carrasco D., Gruda M., Ryan C., Lira S.A., Bravo R. Disruption of the erp/mkp-1 gene does not affect mouse development: normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene. 13:1996;925-931.
-
(1996)
Oncogene
, vol.13
, pp. 925-931
-
-
Dorfman, K.1
Carrasco, D.2
Gruda, M.3
Ryan, C.4
Lira, S.A.5
Bravo, R.6
-
21
-
-
0028157519
-
MSG5, a novel protein phosphatase promotes adaptation to pheromone
-
Doi K., Gartner A., Ammerer G., Errede B., Shinkawa H., Sugimoto K., Matsumoto K. MSG5, a novel protein phosphatase promotes adaptation to pheromone. EMBO J. 13:1994;61-70.
-
(1994)
EMBO J
, vol.13
, pp. 61-70
-
-
Doi, K.1
Gartner, A.2
Ammerer, G.3
Errede, B.4
Shinkawa, H.5
Sugimoto, K.6
Matsumoto, K.7
-
22
-
-
0030660201
-
Derepressed hyphal growth and reduced virulence in a VH1 family-related protein phosphatase mutant of the human pathogen Candida albicans
-
Csank C., Makris C., Meloche S., Schroppel K., Rollinghoff M., Dignard D., Thomas D.Y., Whiteway M. Derepressed hyphal growth and reduced virulence in a VH1 family-related protein phosphatase mutant of the human pathogen Candida albicans. Mol Biol Cell. 8:1997;2539-2551.
-
(1997)
Mol Biol Cell
, vol.8
, pp. 2539-2551
-
-
Csank, C.1
Makris, C.2
Meloche, S.3
Schroppel, K.4
Rollinghoff, M.5
Dignard, D.6
Thomas, D.Y.7
Whiteway, M.8
-
23
-
-
0032472327
-
+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast
-
+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase phosphatase in fission yeast. EMBO J. 17:1998;140-148.
-
(1998)
EMBO J
, vol.17
, pp. 140-148
-
-
Sugiura, R.1
Toda, T.2
Shuntoh, H.3
Yanagida, M.4
Kuno, T.5
-
24
-
-
0029824847
-
A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila
-
Sluss H.K., Han Z., Barret T., Davis R.J., Ip Y.T. A JNK signal transduction pathway that mediates morphogenesis and an immune response in Drosophila. Genes Dev. 10:1996;2745-2758.
-
(1996)
Genes Dev
, vol.10
, pp. 2745-2758
-
-
Sluss, H.K.1
Han, Z.2
Barret, T.3
Davis, R.J.4
Ip, Y.T.5
-
25
-
-
0027884890
-
Puckered, a gene involved in position-specific cell differentiation in the dorsal epidermis
-
Ring J.M., Martinez-Arias A. puckered, a gene involved in position-specific cell differentiation in the dorsal epidermis. Development. 19:1993;251-259.
-
(1993)
Development
, vol.19
, pp. 251-259
-
-
Ring, J.M.1
Martinez-Arias, A.2
-
26
-
-
0032519787
-
Puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila
-
This paper provides the first direct in vivo evidence for a dual specificity phosphatase regulating a MAPK signalling pathway in higher eukaryotes; it also demonstrates that this enzyme functions in a negative feedback loop to regulate Drosophila JNK activity
-
Martin-Blanco E., Gampel A., Ring J., Virdee K., Kirov N., Tolkovsky A.M., Martinez Arias A. puckered encodes a phosphatase that mediates a feedback loop regulating JNK activity during dorsal closure in Drosophila. Genes Dev. 12:1998;557-570. This paper provides the first direct in vivo evidence for a dual specificity phosphatase regulating a MAPK signalling pathway in higher eukaryotes; it also demonstrates that this enzyme functions in a negative feedback loop to regulate Drosophila JNK activity.
-
(1998)
Genes Dev
, vol.12
, pp. 557-570
-
-
Martin-Blanco, E.1
Gampel, A.2
Ring, J.3
Virdee, K.4
Kirov, N.5
Tolkovsky, A.M.6
Martinez Arias, A.7
-
27
-
-
0031027466
-
Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein-kinase by the PTP2 and PTP3 protein-tyrosine phosphatases
-
Wurgler-Murphy S.M., Maeda T., Witten E.A., Saito H. Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein-kinase by the PTP2 and PTP3 protein-tyrosine phosphatases. Mol Cell Biol. 17:1997;1289-1297.
-
(1997)
Mol Cell Biol
, vol.17
, pp. 1289-1297
-
-
Wurgler-Murphy, S.M.1
Maeda, T.2
Witten, E.A.3
Saito, H.4
-
28
-
-
0030760722
-
2 protein-tyrosine phosphatases inactivate the osmotic-stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1
-
Jacoby T., Flanagan H., Faykin A., Seto A.G., Mattison C., Ota I. 2 protein-tyrosine phosphatases inactivate the osmotic-stress response pathway in yeast by targeting the mitogen-activated protein kinase, Hog1. J Biol Chem. 272:1997;17749-17755.
-
(1997)
J Biol Chem
, vol.272
, pp. 17749-17755
-
-
Jacoby, T.1
Flanagan, H.2
Faykin, A.3
Seto, A.G.4
Mattison, C.5
Ota, I.6
-
29
-
-
0030820725
-
Differential regulation of FUS3 map kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase Msg5 in Saccharomyces-cerevisiae
-
Zhan X.L., Deschenes R.J., Guan K.L. Differential regulation of FUS3 map kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase Msg5 in Saccharomyces-cerevisiae. Genes Dev. 11:1997;1690-1702.
-
(1997)
Genes Dev
, vol.11
, pp. 1690-1702
-
-
Zhan, X.L.1
Deschenes, R.J.2
Guan, K.L.3
-
30
-
-
0029089795
-
Pyp1 and pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell-size at division in fission yeast
-
Millar J.B.A., Buck V., Wilkinson M.G. Pyp1 and pyp2 PTPases dephosphorylate an osmosensing MAP kinase controlling cell-size at division in fission yeast. Genes Dev. 9:1995;2117-2130.
-
(1995)
Genes Dev
, vol.9
, pp. 2117-2130
-
-
Millar, J.B.A.1
Buck, V.2
Wilkinson, M.G.3
-
31
-
-
0029563651
-
Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast
-
Shiozaki K., Russell P. Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast. Nature. 378:1995;739-743.
-
(1995)
Nature
, vol.378
, pp. 739-743
-
-
Shiozaki, K.1
Russell, P.2
-
32
-
-
0032534791
-
PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
-
This paper identifies a new class of tyrosine-specific phosphatases which regulate MAPK in mammalian cells. It also defines an interaction motif within the amini-terminal noncatalytic domain of these enzymes, which mediates ERK binding
-
Pulido R., Zuniga A., Ullrich A. PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J. 17:1998;7337-7350. This paper identifies a new class of tyrosine-specific phosphatases which regulate MAPK in mammalian cells. It also defines an interaction motif within the amini-terminal noncatalytic domain of these enzymes, which mediates ERK binding.
-
(1998)
EMBO J
, vol.17
, pp. 7337-7350
-
-
Pulido, R.1
Zuniga, A.2
Ullrich, A.3
-
33
-
-
0033525793
-
Inactivation of mitogen-activated protein kinases by a mammalian tyrosine-specific enzyme
-
Ogata M., Oh-hora M., Kosugi A., Hamaoka T. Inactivation of mitogen-activated protein kinases by a mammalian tyrosine-specific enzyme. Biochem Biophys Res Commun. 256:1999;52-55.
-
(1999)
Biochem Biophys Res Commun
, vol.256
, pp. 52-55
-
-
Ogata, M.1
Oh-Hora, M.2
Kosugi, A.3
Hamaoka, T.4
-
34
-
-
0032546961
-
Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)
-
Saxena M., Williams S., Gilman J., Mustelin T. Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP). J Biol Chem. 273:1998;15340-15344.
-
(1998)
J Biol Chem
, vol.273
, pp. 15340-15344
-
-
Saxena, M.1
Williams, S.2
Gilman, J.3
Mustelin, T.4
-
35
-
-
0033597122
-
Inhibition of T cell signalling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)
-
This paper identifies the target for HePTP in mediating suppression of antigen receptor-induced transcription from the interleukin gene promoter as ERK1 and ERK2
-
Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T. Inhibition of T cell signalling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP). J Biol Chem. 274:1999;11693-11700. This paper identifies the target for HePTP in mediating suppression of antigen receptor-induced transcription from the interleukin gene promoter as ERK1 and ERK2.
-
(1999)
J Biol Chem
, vol.274
, pp. 11693-11700
-
-
Saxena, M.1
Williams, S.2
Brockdorff, J.3
Gilman, J.4
Mustelin, T.5
-
36
-
-
0033178615
-
Direct suppression of TCR-mediated activation of extracellular signal-regulated kinase by leukocyte protein tyrosine phosphatase, a tyrosine-specific phosphatase
-
This paper identifies ERK1 and ERK2 as substrates for leukocyte PTP but also shows that this phospatase is unable to interact with or inactivate the sevenmaker ERK2 gain-of-function mutant
-
Oh-hora M., Ogata M., Mori Y., Adachi M., Imai K., Kosugi A., Hamaoka T. Direct suppression of TCR-mediated activation of extracellular signal-regulated kinase by leukocyte protein tyrosine phosphatase, a tyrosine-specific phosphatase. J Immunol. 163:1999;1282-1288. This paper identifies ERK1 and ERK2 as substrates for leukocyte PTP but also shows that this phospatase is unable to interact with or inactivate the sevenmaker ERK2 gain-of-function mutant.
-
(1999)
J Immunol
, vol.163
, pp. 1282-1288
-
-
Oh-Hora, M.1
Ogata, M.2
Mori, Y.3
Adachi, M.4
Imai, K.5
Kosugi, A.6
Hamaoka, T.7
-
37
-
-
0038845769
-
Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm
-
Zuniga A., Torres J., Ubeda J., Pulido R. Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm. J Biol Chem. 274:1999;21900-21907.
-
(1999)
J Biol Chem
, vol.274
, pp. 21900-21907
-
-
Zuniga, A.1
Torres, J.2
Ubeda, J.3
Pulido, R.4
-
38
-
-
0033193930
-
Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase
-
This paper indicates that crosstalk between the cAMP and MAPK signaling pathway may be mediated via phosphorylation of HePTP by protein kinase A, leading to dissociation of the complex between HePTP and its MAPK substrate
-
Saxena M., Williams S., Tasken K., Mustelin T. Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase. Nat Cell Biol. 1:1999;305-311. This paper indicates that crosstalk between the cAMP and MAPK signaling pathway may be mediated via phosphorylation of HePTP by protein kinase A, leading to dissociation of the complex between HePTP and its MAPK substrate.
-
(1999)
Nat Cell Biol
, vol.1
, pp. 305-311
-
-
Saxena, M.1
Williams, S.2
Tasken, K.3
Mustelin, T.4
-
39
-
-
0028840142
-
A neuronal protein tyrosine phosphatase induced by nerve growth factor
-
Sharma E., Lombroso P.J. A neuronal protein tyrosine phosphatase induced by nerve growth factor. Proc Natl Acad Sci USA. 270:1995;49-53.
-
(1995)
Proc Natl Acad Sci USA
, vol.270
, pp. 49-53
-
-
Sharma, E.1
Lombroso, P.J.2
-
40
-
-
0033153370
-
PTP-ER, a novel tyrosine phospatase, functions downstream of Ras1 to downregulate MAP kinase during Drosophila eye development
-
A genetic screen is used to isolate a novel protein tyrosine phosphatase PTP-ER, which dephosphorylates and inactivates MAP kinase in vitro and in vivo. This study provides direct in vivo evidence for a tyrosine-specific phosphatase regulating ERK/MAPK in higher eukaroytes
-
Karim F.D., Rubin G.M. PTP-ER, a novel tyrosine phospatase, functions downstream of Ras1 to downregulate MAP kinase during Drosophila eye development. Mol Cell. 3:1999;741-750. A genetic screen is used to isolate a novel protein tyrosine phosphatase PTP-ER, which dephosphorylates and inactivates MAP kinase in vitro and in vivo. This study provides direct in vivo evidence for a tyrosine-specific phosphatase regulating ERK/MAPK in higher eukaroytes.
-
(1999)
Mol Cell
, vol.3
, pp. 741-750
-
-
Karim, F.D.1
Rubin, G.M.2
-
41
-
-
0033532067
-
Extracellular regulated kinases (ERK)1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR
-
Todd J.L., Tanner K.G., Denu J.M. Extracellular regulated kinases (ERK)1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. 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
-
42
-
-
0029257329
-
Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100 in various cell lines
-
Alessi D.R., Gomez N., Moorhead G., Lewis T., Keyse S.M., Cohen P. Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100 in various cell lines. Curr Biol. 5:1995;283-295.
-
(1995)
Curr Biol
, vol.5
, pp. 283-295
-
-
Alessi, D.R.1
Gomez, N.2
Moorhead, G.3
Lewis, T.4
Keyse, S.M.5
Cohen, P.6
-
43
-
-
0032541227
-
Protein phosphatase 2Cα inhibits the human stress-responsive p38 and JNK MAPK pathways
-
Takekawa T., Maeda T., Saito H. Protein phosphatase 2Cα inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J. 17:1998;4744-4752.
-
(1998)
EMBO J
, vol.17
, pp. 4744-4752
-
-
Takekawa, T.1
Maeda, T.2
Saito, H.3
-
44
-
-
0033081066
-
Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry
-
Brunet A., Roux D., Lenormand P., Dowd S., Keyse S.M., Pouyssegur J. Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry. EMBO J. 18:1999;664-674.
-
(1999)
EMBO J
, vol.18
, pp. 664-674
-
-
Brunet, A.1
Roux, D.2
Lenormand, P.3
Dowd, S.4
Keyse, S.M.5
Pouyssegur, J.6
-
45
-
-
0028328631
-
A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase pathways
-
Brunner D., Oellers N., Szabad J., Briggs W.H., Zipursky S.L., Hafen E. A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase pathways. Cell. 76:1994;875-888.
-
(1994)
Cell
, vol.76
, pp. 875-888
-
-
Brunner, D.1
Oellers, N.2
Szabad, J.3
Briggs, W.H.4
Zipursky, S.L.5
Hafen, E.6
-
46
-
-
0028145758
-
The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual-specificity phosphatase action
-
Bott C.M., Thorneycroft S.G., Marshall C.J. The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual-specificity phosphatase action. FEBS Lett. 352:1995;201-205.
-
(1995)
FEBS Lett
, vol.352
, pp. 201-205
-
-
Bott, C.M.1
Thorneycroft, S.G.2
Marshall, C.J.3
-
47
-
-
0029918680
-
The mitogen-activated protein kinase phosphatases PAC1, MKP-1 and MKP-2 have unique substrate specificities and reduced activity in vivo towards the ERK2 sevenmaker mutation
-
Chu Y., Solski P.A., Khosravi-Far R., Der C.J., Kelly K. The mitogen-activated protein kinase phosphatases PAC1, MKP-1 and MKP-2 have unique substrate specificities and reduced activity in vivo towards the ERK2 sevenmaker mutation. J Biol Chem. 271:1996;6497-6501.
-
(1996)
J Biol Chem
, vol.271
, pp. 6497-6501
-
-
Chu, Y.1
Solski, P.A.2
Khosravi-Far, R.3
Der, C.J.4
Kelly, K.5
-
48
-
-
0038832564
-
MAPK-dependent phosphorylation
-
MAPK led to stabilisation of the protein. These results reveal a new facet of a complex control mechanism which is designed to prevent the undesirable effects of long-term activation of these key mitogenic signalling pathways
-
MAPK led to stabilisation of the protein. These results reveal a new facet of a complex control mechanism which is designed to prevent the undesirable effects of long-term activation of these key mitogenic signalling pathways.
-
(1999)
Science
, vol.286
, pp. 2514-2517
-
-
Brondello, J.-M.1
Pouyssegur, J.2
McKenzie, F.R.3
-
49
-
-
0032700045
-
A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase
-
Tyrosine specific MKPs are found in both S. cerevisiae and mammalian cells. However, the kinase interaction motif (KIM) identified in the non-catalytic amino terminus of the mammalian enzymes, which is responsible for MAPK binding, is not present in yeast phosphatases such as Ptp3p which targets the Fus3p MAP kinase. Here the authors demonstrate that Ptp3p does bind to its substrate Fus3p via its non-catalytic amino-terminal domain. However, the sequence motif responsible is more similar to those identified in the non-catalytic amino terminal domains of the mammalian dual-specificity MKPs. This paper reinforces the concept that the specificity of MAP kinase inactivation in vivo is governed by specific protein-protein interactions with the phiosphatase catalytic domain
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Zhan X-L., Guan K.L. A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase. Genes Dev. 13:1999;2811-2827. Tyrosine specific MKPs are found in both S. cerevisiae and mammalian cells. However, the kinase interaction motif (KIM) identified in the non-catalytic amino terminus of the mammalian enzymes, which is responsible for MAPK binding, is not present in yeast phosphatases such as Ptp3p which targets the Fus3p MAP kinase. Here the authors demonstrate that Ptp3p does bind to its substrate Fus3p via its non-catalytic amino-terminal domain. However, the sequence motif responsible is more similar to those identified in the non-catalytic amino terminal domains of the mammalian dual-specificity MKPs. This paper reinforces the concept that the specificity of MAP kinase inactivation in vivo is governed by specific protein-protein interactions with the phiosphatase catalytic domain.
-
(1999)
Genes Dev
, vol.13
, pp. 2811-2827
-
-
Zhan, X.-L.1
Guan, K.L.2
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