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0032928614
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Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
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Widmann C., Gibson S., Jarpe M.B., Johnson G.L. Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human. Physiol Rev. 79:1999;143-180.
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Widmann, C.1
Gibson, S.2
Jarpe, M.B.3
Johnson, G.L.4
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0032422785
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Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
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Whitmarsh A.J., Davis R.J. Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem Sci. 23:1998;481-485.
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Trends Biochem Sci
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Whitmarsh, A.J.1
Davis, R.J.2
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Organization of kinases, phosphatases, and receptor signaling complexes
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Schillace R.V., Scott J.D. Organization of kinases, phosphatases, and receptor signaling complexes. J Clin Invest. 103:1999;761-765.
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J Clin Invest
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Schillace, R.V.1
Scott, J.D.2
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4
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0032935664
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Mitogen-activated protein kinases: Specific messages from ubiquitous messengers
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This is a general review that also touches on the utility of scaffolds in the regulation of signal transduction.
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Schaeffer H.J., Weber M.J. Mitogen-activated protein kinases: specific messages from ubiquitous messengers. Mol Cel Biol. 19:1999;2435-2444. This is a general review that also touches on the utility of scaffolds in the regulation of signal transduction.
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(1999)
Mol Cel Biol
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, pp. 2435-2444
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Schaeffer, H.J.1
Weber, M.J.2
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0031457622
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Signaling through scaffold, anchoring, and adaptor proteins
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Pawson T., Scott J.D. Signaling through scaffold, anchoring, and adaptor proteins. Science. 278:1997;2075-2080.
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Science
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Pawson, T.1
Scott, J.D.2
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0032910168
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Organization and regulation of mitogen-activated protein kinase signaling pathways
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This is a succint and complete review, published recently, which includes extensive lists of proposed MAPK pathway scaffolds and their ligands.
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Garrington T.P., Johnson G.L. Organization and regulation of mitogen-activated protein kinase signaling pathways. Curr Opin Cell Biol. 11:1999;211-218. This is a succint and complete review, published recently, which includes extensive lists of proposed MAPK pathway scaffolds and their ligands.
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Curr Opin Cell Biol
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Garrington, T.P.1
Johnson, G.L.2
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0027983908
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Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae
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Choi K.Y., Satterberg Lyons D.M., Elion E.A. Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae. Cell. 78:1994;499-512.
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Cell
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Choi, K.Y.1
Satterberg Lyons, D.M.2
Elion, E.A.3
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8
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0027991228
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Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module
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Marcus S., Polverino A., Barr M., Wigler M. Complexes between STE5 and components of the pheromone-responsive mitogen-activated protein kinase module. Proc Natl Acad Sci USA. 91:1994;7762-7766.
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Proc Natl Acad Sci USA
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Marcus, S.1
Polverino, A.2
Barr, M.3
Wigler, M.4
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9
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0032694245
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JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a scaffold factor in the JNK signaling pathway
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Using a yeast two-hybrid approach, the authors identify a 145 kDa protein that associates with JNKs 1,2, and 3, as well as SEK1 (a JNK kinase) and MEKK1, suggesting that it acts as a scaffold for the JNK/SAPK pathway. There is no homology between this molecule and the previously described JIPs.
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Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.I. JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a scaffold factor in the JNK signaling pathway. Mol Cell Biol. 19:1999;7539-7548. Using a yeast two-hybrid approach, the authors identify a 145 kDa protein that associates with JNKs 1,2, and 3, as well as SEK1 (a JNK kinase) and MEKK1, suggesting that it acts as a scaffold for the JNK/SAPK pathway. There is no homology between this molecule and the previously described JIPs.
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Mol Cell Biol
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, pp. 7539-7548
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Ito, M.1
Yoshioka, K.2
Akechi, M.3
Yamashita, S.4
Takamatsu, N.5
Sugiyama, K.6
Hibi, M.7
Nakabeppu, Y.8
Shiba, T.9
Yamamoto, K.I.10
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10
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0030835610
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A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade
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Tsunoda S., Sierralta J., Sun Y.M., Bodner R., Suzuki E., Becker A., Socolich M., Zuker C.S. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade. Nature. 388:1997;243-249.
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Nature
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Tsunoda, S.1
Sierralta, J.2
Sun, Y.M.3
Bodner, R.4
Suzuki, E.5
Becker, A.6
Socolich, M.7
Zuker, C.S.8
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11
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0033516701
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Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex
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Yotiao is identified as an anchoring protein binding both a phosphatase, PP1, and the RII subunit of protein kinase A (PKA). PP1 acts constituitively on the NMDA-receptor, maintaining it in an inactive state. cAMP association with RII allows dissociation of the catalytic subunit, which is presumed to allow phosphorylation of the NMDA receptor, apparently overcoming the low rate of phosphatase activity.
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Westphal R.S., Tavalin S.J., Lin J.W., Alto N.M., Fraser I.D.C., Langeberg L.K., Sheng M., Scott J.D. Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex. Science. 285:1999;93-96. Yotiao is identified as an anchoring protein binding both a phosphatase, PP1, and the RII subunit of protein kinase A (PKA). PP1 acts constituitively on the NMDA-receptor, maintaining it in an inactive state. cAMP association with RII allows dissociation of the catalytic subunit, which is presumed to allow phosphorylation of the NMDA receptor, apparently overcoming the low rate of phosphatase activity.
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(1999)
Science
, vol.285
, pp. 93-96
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Westphal, R.S.1
Tavalin, S.J.2
Lin, J.W.3
Alto, N.M.4
Fraser, I.D.C.5
Langeberg, L.K.6
Sheng, M.7
Scott, J.D.8
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12
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0033534533
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Adaptors and molecular scaffolds in immune cell signaling
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Rudd C.E. Adaptors and molecular scaffolds in immune cell signaling. Cell. 96:1999;5-8.
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(1999)
Cell
, vol.96
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Rudd, C.E.1
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13
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0032558776
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Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses
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Assessing signal transduction from a single rhodopsin and with millisecond resolution, the authors exploit several Drosphila mutants to show that amplification does not occur within the scaffolded portion of the signal transduction cascade.
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Scott K., Zuker C.S. Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses. Nature. 395:1998;805-808. Assessing signal transduction from a single rhodopsin and with millisecond resolution, the authors exploit several Drosphila mutants to show that amplification does not occur within the scaffolded portion of the signal transduction cascade.
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(1998)
Nature
, vol.395
, pp. 805-808
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Scott, K.1
Zuker, C.S.2
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14
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0032496358
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The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
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This work suggests that a 'switch-like' cellular response (germinal vesicle breakdown) has its origin in the character of MAPK signal transduction pathway.
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Ferrell J.E., Machleder E.M. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science. 280:1998;895-898. This work suggests that a 'switch-like' cellular response (germinal vesicle breakdown) has its origin in the character of MAPK signal transduction pathway.
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(1998)
Science
, vol.280
, pp. 895-898
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Ferrell, J.E.1
Machleder, E.M.2
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15
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Ultrasensitivity in the mitogen-activated protein kinase cascade
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Huang C.Y., Ferrell J.E. Jr. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc Natl Acad Sci USA. 93:1996;10078-10083.
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Proc Natl Acad Sci USA
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Huang, C.Y.1
Ferrell J.E., Jr.2
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16
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0030746219
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Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase
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Ferrell J.E., Bhatt R.R. Mechanistic studies of the dual phosphorylation of mitogen-activated protein kinase. J Biol Chem. 272:1997;19008-19016.
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J Biol Chem
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Ferrell, J.E.1
Bhatt, R.R.2
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17
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0030972112
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The activating dual phosphorylation of MAPK by MEK is nonprocessive
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Burack W.R., Sturgill T.W. The activating dual phosphorylation of MAPK by MEK is nonprocessive. Biochemistry. 36:1997;5929-5933.
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(1997)
Biochemistry
, vol.36
, pp. 5929-5933
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Burack, W.R.1
Sturgill, T.W.2
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18
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0030450397
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Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction
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Yablonski D., Marbach I., Levitzki A. Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction. Proc Natl Acad Sci USA. 93:1996;13864-13869.
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Proc Natl Acad Sci USA
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, pp. 13864-13869
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Yablonski, D.1
Marbach, I.2
Levitzki, A.3
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19
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0030815533
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Ste5 ring-H2 domain - role in Ste4-promoted oligomerization for yeast pheromone signaling
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Inouye C., Dhillon N., Thorner J. Ste5 ring-H2 domain - role in Ste4-promoted oligomerization for yeast pheromone signaling. Science. 278:1997;103-106.
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(1997)
Science
, vol.278
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Inouye, C.1
Dhillon, N.2
Thorner, J.3
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20
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0033588242
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Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade
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The authors exploit an array of yeast mutants to probe the trafficking of sterile 5 (Ste5). In one striking experiment using temperature-sensitive export mutants, they show that only Ste5 that has recently passed through the nucleus is competent to support transduction. The results suggest that Ste5 undergoes some modification within the nucleus and the authors propose that phosphorylation may be the modification.
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Mahanty S.K., Wang Y.M., Farley F.W., Elion E.A. Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade. Cell. 98:1999;501-512. The authors exploit an array of yeast mutants to probe the trafficking of sterile 5 (Ste5). In one striking experiment using temperature-sensitive export mutants, they show that only Ste5 that has recently passed through the nucleus is competent to support transduction. The results suggest that Ste5 undergoes some modification within the nucleus and the authors propose that phosphorylation may be the modification.
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(1999)
Cell
, vol.98
, pp. 501-512
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Mahanty, S.K.1
Wang, Y.M.2
Farley, F.W.3
Elion, E.A.4
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21
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0032959886
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Identification of constitutive and Ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression
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The authors demonstrate that overexpression of KSR inhibits Ras signal transduction, although this molecule was identified by genetic means as a mediator of Ras signalling.
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Cacace A.M., Michaud N.R., Therrien M., Mathes K., Copeland T., Rubin G.M., Morrison D.K. Identification of constitutive and Ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol Cell Biol. 19:1999;229-240. The authors demonstrate that overexpression of KSR inhibits Ras signal transduction, although this molecule was identified by genetic means as a mediator of Ras signalling.
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(1999)
Mol Cell Biol
, vol.19
, pp. 229-240
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Cacace, A.M.1
Michaud, N.R.2
Therrien, M.3
Mathes, K.4
Copeland, T.5
Rubin, G.M.6
Morrison, D.K.7
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22
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0031974151
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Murine Ksr interacts with Mek and inhibits Ras-induced transformation
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Denouelgaly A., Douville E.M., Warne P.H., Papin C., Laugier D., Calothy G., Downward J., Eychene A. Murine Ksr interacts with Mek and inhibits Ras-induced transformation. Curr Biol. 8:1998;46-55.
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(1998)
Curr Biol
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Denouelgaly, A.1
Douville, E.M.2
Warne, P.H.3
Papin, C.4
Laugier, D.5
Calothy, G.6
Downward, J.7
Eychene, A.8
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23
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0032814144
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Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization
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The authors show that kinase-negative KSR can complement a KSR-deficient phenotype in Caenorhabditis elegans, implying that catalytic function is not necessary for this activity. Furthermore, KSR in cell lysates is present in large (~700 kDa) aggregates as determined by gel filtration. Co-immunoprecipitation experiments suggest that these aggregates also contain MEK1 and 2, Hsp70, Hsp68, Hsp90 and p50cdc37. Smaller amounts of ERK and even Raf were detected in these co-immunoprecipitations. KSR expression induced the translocation of MEK from a soluble (S-100) to a presumably membrane-associated cell fraction (P-100). There was no evidence of formation of KSR oligomers.
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Stewart S., Sundaram M., Zhang Y.P., Lee J.Y., Han M., Guan K.L. Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. Mol Cell Biol. 19:1999;5523-5534. The authors show that kinase-negative KSR can complement a KSR-deficient phenotype in Caenorhabditis elegans, implying that catalytic function is not necessary for this activity. Furthermore, KSR in cell lysates is present in large (~700 kDa) aggregates as determined by gel filtration. Co-immunoprecipitation experiments suggest that these aggregates also contain MEK1 and 2, Hsp70, Hsp68, Hsp90 and p50cdc37. Smaller amounts of ERK and even Raf were detected in these co-immunoprecipitations. KSR expression induced the translocation of MEK from a soluble (S-100) to a presumably membrane-associated cell fraction (P-100). There was no evidence of formation of KSR oligomers.
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(1999)
Mol Cell Biol
, vol.19
, pp. 5523-5534
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Stewart, S.1
Sundaram, M.2
Zhang, Y.P.3
Lee, J.Y.4
Han, M.5
Guan, K.L.6
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24
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0032536853
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The kinase suppressor of Ras (Ksr) modulates growth factor and ras signaling by uncoupling elk-1 phosphorylation from map kinase activation
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While the inhibition observed with overexpression of KSR superficially is consistent with a scaffold function, the authors find that the inhibition does not occur within the scaffolded portion of the pathway. Rather phosphorylation of the transcription factor ELK, an ERK substrate, is inhibited rather than activation of ERK itself.
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Sugimoto T., Stewart S., Han M., Guan K.L. The kinase suppressor of Ras (Ksr) modulates growth factor and ras signaling by uncoupling elk-1 phosphorylation from map kinase activation. EMBO J. 17:1998;1717-1727. While the inhibition observed with overexpression of KSR superficially is consistent with a scaffold function, the authors find that the inhibition does not occur within the scaffolded portion of the pathway. Rather phosphorylation of the transcription factor ELK, an ERK substrate, is inhibited rather than activation of ERK itself.
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(1998)
EMBO J
, vol.17
, pp. 1717-1727
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Sugimoto, T.1
Stewart, S.2
Han, M.3
Guan, K.L.4
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25
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0031974812
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Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with Mek and Erk
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Yu W., Fantl W.J., Harrowe G., Williams L.T. Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with Mek and Erk. Curr Biol. 8:1998;56-64.
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(1998)
Curr Biol
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, pp. 56-64
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Yu, W.1
Fantl, W.J.2
Harrowe, G.3
Williams, L.T.4
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26
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0029586594
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KSR: A novel player in the RAS pathway
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Downward J. KSR: a novel player in the RAS pathway. Cell. 83:1995;831-834.
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Cell
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Downward, J.1
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27
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0032541670
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Ikap is a scaffold protein of the I-kappa-B kinase complex
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Using affinity purification techniques, the authors identified a 150 kDa protein with five WD domains. Termed 'inhibitory kinase associated protein' (IKAP), it binds three kinases that in turn regulate an inhibitor of NF-κB. Association with IKAP altered the activities of the three kinases. The authors used inhibition of signal with overexpression of IKAP as a criterion for identifying this protein as a scaffold.
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Cohen L., Henzel W.J., Baeuerle P.A. Ikap is a scaffold protein of the I-kappa-B kinase complex. Nature. 395:1998;292-296. Using affinity purification techniques, the authors identified a 150 kDa protein with five WD domains. Termed 'inhibitory kinase associated protein' (IKAP), it binds three kinases that in turn regulate an inhibitor of NF-κB. Association with IKAP altered the activities of the three kinases. The authors used inhibition of signal with overexpression of IKAP as a criterion for identifying this protein as a scaffold.
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(1998)
Nature
, vol.395
, pp. 292-296
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Cohen, L.1
Henzel, W.J.2
Baeuerle, P.A.3
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28
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0032508714
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Mammalian scaffold complex that selectively mediates MAP kinase activation
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Using overexpression methods described in a previous study, this protein was identified as an inhibitor of a MAPK pathway. In this study, overexpression of JIP-1 is seen to enhance signal transduction when its ligand proteins are also overexpressed.
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Whitmarsh A.J., Cavanagh L., Tournier C., Yasuda L., Davis R.J. Mammalian scaffold complex that selectively mediates MAP kinase activation. Science. 281:1998;1671-1674. Using overexpression methods described in a previous study, this protein was identified as an inhibitor of a MAPK pathway. In this study, overexpression of JIP-1 is seen to enhance signal transduction when its ligand proteins are also overexpressed.
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(1998)
Science
, vol.281
, pp. 1671-1674
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Whitmarsh, A.J.1
Cavanagh, L.2
Tournier, C.3
Yasuda, L.4
Davis, R.J.5
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29
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0032508538
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Mp1 - A Mek binding partner that enhances enzymatic activation of the Map kinase cascade
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Using a yeast-two hybrid approach, the authors identify a protein that binds both MEK and ERK. The authors indicate that it is difficult to show a positive effect on signal transduction in overexpression systems unless ERK and MEK are simultaneously overexpressed. These data correlate well with those expected for a simple passive scaffold.
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Schaeffer H.J., Catling A.D., Eblen S.T., Collier L.S., Krauss A., Weber M.J. Mp1 - a Mek binding partner that enhances enzymatic activation of the Map kinase cascade. Science. 281:1998;1668-1671. Using a yeast-two hybrid approach, the authors identify a protein that binds both MEK and ERK. The authors indicate that it is difficult to show a positive effect on signal transduction in overexpression systems unless ERK and MEK are simultaneously overexpressed. These data correlate well with those expected for a simple passive scaffold.
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(1998)
Science
, vol.281
, pp. 1668-1671
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Schaeffer, H.J.1
Catling, A.D.2
Eblen, S.T.3
Collier, L.S.4
Krauss, A.5
Weber, M.J.6
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Identification of MAP kinase domains by redirecting stress signals into growth factor responses
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Brunet A., Pouyssegur J. Identification of MAP kinase domains by redirecting stress signals into growth factor responses. Science. 272:1996;1652-1655.
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Science
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Brunet, A.1
Pouyssegur, J.2
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