| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.63919501 |
| The inability of MKP 2 to dephosphorylate ERK in vivo is also not due to the inability of Flag MKP 2 to bind both ERK and JNK ; phosphorylated forms of each kinase are co precipitated with both WT and CI MKP 2 . 0.63919501^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The mitogen activated protein kinase phosphatases PAC 1 , MKP 1 , and MKP 2 have unique substrate specificities and reduced activity in vivo toward the ERK 2 sevenmaker mutation . ^^^ PAC 1 , MKP 2 , and MKP 1 recognize ERK and p 38 , ERK and JNK , and ERK , p 38 , and JNK , respectively . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The mitogen activated protein kinase ( MAPK ) phosphatase MKP 2 [ inactivates extracellular regulated kinase ( ERK ) = Jun N terminal kinase ( JNK ) > p 38 MAPK ] completely abrogates MMP 1 activation , whereas PAC 1 ( inactivates ERK = p 38 > JNK ) attenuates but does not completely prevent induction . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The SCN expressed both nuclear MAPK phosphatases ( MKP 1 and MKP 2 ) and the cytosolic MAPK phosphatase Mkp 3 , thus providing mechanisms by which light induced ERK activation is terminated . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Taken together , these data indicate that the increased level and activity of MKP 2 in senescent WI 38 cells are the consequence of impaired proteosomal degradation , and this increase is likely to play a significant role in the decreased levels of p ERK in the nucleus of senescent cells . . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| This delayed repression of JNK was preceded by phosphorylation of the MKP 2 phosphatase , and both MKP 2 induction and JNK dephosphorylation were under the control of MEK , the upstream kinase of ERK . ^^^ ERK and MKP 2 stimulate the EBS / AP1 dependent transcriptional response to SF / HGF , but not JNK , which inhibits this response . ^^^ We further demonstrated that depending on cell density , the RAS ERK MKP 2 pathway controls this transrepressing effect of JNK . ^^^ Together , these data demonstrate that in a sequential manner SF / HGF activates ERK and MKP 2 , which in turn dephosphorylates JNK . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Although MKP 2 preferentially inactivates extracellular signal regulated kinase ( ERK ) and c Jun NH ( 2 ) terminal kinase ( JNK ) MAP kinase subfamilies , the mechanisms underlying its own regulation remain unclear . ^^^ We found that the catalytic activity of MKP 2 was enhanced dramatically by ERK and JNK but was affected only minimally by p 38 . ^^^ By contrast , p 38 and ERK bound MKP 2 with comparably strong affinities , whereas JNK and MKP 2 interacted very weakly . ^^^ Through site directed mutagenesis , we defined the ERK / p38 binding site as a cluster of arginine residues in the NH ( 2 ) terminal domain of MKP 2 . ^^^ Mutation of the basic motif abrogated its interaction with both ERK and p 38 and severely compromised the catalytic activation of MKP 2 by these kinases . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Functional analysis of the MKP 2 promoter confirmed a requirement for the protein kinase C extracellular signal regulated kinase ( ERK ) pathway and VGCC derived Ca ( 2+ ) signals in transcriptional activation of the MKP 2 gene . ^^^ MGRE ( MKP 2 GnRH response element ) within the MKP 2 promoter mediated promoter activation through the protein kinase C ERK pathway . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The 1 ( 1 ) imidazoline receptor in PC 12 pheochromocytoma cells reverses NGF induced ERK activation and induces MKP 2 phosphatase . ^^^ Therefore , we assayed levels of MKP 2 , a dual specificity phosphatase whose substrates include ERK . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| We measured sexual behaviors and brain levels of ERK , phosphorylated ERK ( pERK ) , protein phosphatase 1 ( PP 1 ) , and MAPK phosphatase 2 ( MKP 2 ) during adulthood in control and neonatally CLI treated rats ( CLI rats ) . ^^^ As expected , the CLI rats exhibited significantly lower sexual activities and also exhibited ( 1 ) . significant decreases of pERK1 / 2 in the frontal cortex and pERK 1 in the hippocampus , ( 2 ) . slight but significant reduction of ERK 2 in the frontal cortex and hippocampus , ( 3 ) . no change of pERK1 / 2 levels in the temporal cortex , occipital cortex , parietal cortex , midbrain , and medulla , ( 4 ) . significantly higher levels of PP 1 in both the frontal cortex and hippocampus , ( 5 ) . no change in MKP 2 in any examined region , and ( 6 ) . all five measures of sexual function were significantly correlated with ERK 2 and pERK 2 in the frontal cortex . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The inhibition of MKP 2 may have contributed to the enhancement observed by the thiol of mitogen induced ERK phosphorylation . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Elevated activity of MKP 2 in alphaT 3 1 cells , through either overexpression or activation of the endogenous MKP 2 gene , was correlated with inhibition of GnRH induced activation of ERK and JNK , as well as the expression of ERK and JNK dependent proto oncogenes . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| In normal fibroblasts , the amounts of active MEK and ERK decline at contact inhibition , concurrently with a rise in MKP 1 , MKP 2 , and MKP 3 protein levels . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Recombinant HVH 2 phosphatase exhibited a high substrate specificity toward activated ERK and dephosphorylated both threonine and tyrosine residues of activated ERK 1 and ERK 2 . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| The amount of Smad 2 protein was increased by transfection with a constitutively active MEK 1 and reduced by co transfection with the ERK phosphatase , HVH 2 . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| Isolation and characterisation of a uniquely regulated threonine , tyrosine phosphatase ( TYP 1 ) which inactivates ERK 2 and p54jnk . ^^^ When TYP 1 is transfected into COS 1 cells , the gene product inhibits both ERK 2 and p 54 MAP kinase subfamilies . ^^^ In addition , we show that purified TYP 1 protein efficiently inactivates recombinant ERK 2 in vitro by the concomitant dephosphorylation of both its phosphothreonine and tyrosine residues . ^^^ |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q13115 and P28482 |
Pubmed |
SVM Score :0.0 |
| NA |
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