| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| MEKK 2 associates with the adapter protein Lad / RIBP and regulates the MEK 5 BMK1 / ERK5 pathway . ^^^ By yeast two hybrid library screening , we have identified MEK 5 , the MAPK kinase in the big mitogen activated protein kinase 1 ( BMK 1 ) / ERK5 pathway , as a binding partner for MEKK 2 . ^^^ MEKK 2 expression stimulates BMK1 / ERK5 activity , the downstream substrate for MEK 5 . ^^^ A dominant negative form of MEK 5 blocked the activation of BMK1 / ERK5 by MEKK 2 , whereas activation of c Jun N terminal kinase ( JNK ) was unaffected , showing that MEK 5 is a specific downstream effector of MEKK 2 in the BMK1 / ERK5 pathway . ^^^ MEKK 2 and MEKK 3 are differentially associated with signaling from specific upstream receptor systems , whereas both activate the MEK 5 BMK1 / ERK5 pathway . . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| We describe an alternative pathway by which MEKK 2 activates MEK 5 and big MAP kinase1 / extracellular signal regulated kinase 5 in addition to MKK 7 and JNK , and interruption of this pathway inhibits TNF alpha promoter activation . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| Select point mutations in subdomain 10 impair MEKK 2 phosphorylation of the MAP2Ks , MKK 7 and MEK 5 , abolish MEKK 2 induced activation of the MAPKs , JNK 1 and ERK 5 , and diminish MEKK 2 dependent activation of an AP 1 reporter gene . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| The Phox and Bem1p ( PB 1 ) domain constitutes a recently recognized protein protein interaction domain found in the atypical protein kinase C ( aPKC ) isoenzymes , lambda / iota and zeta PKC ; members of mitogen activated protein kinase ( MAPK ) modules like MEK 5 , MEKK 2 , and MEKK 3 ; and in several scaffold proteins involved in cellular signaling . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| PB 1 domains of MEKK 2 and MEKK 3 interact with the MEK 5 PB1 domain for activation of the ERK 5 pathway . ^^^ MEKK 2 and MEKK 3 are MAPK kinase kinases that activate the ERK 5 pathway by phosphorylating and activating the MAPK kinase , MEK 5 . ^^^ A PB 1 domain is encoded within the N terminal portion of MEKK 2 , MEKK 3 , and MEK 5 . ^^^ Herein , we analyze the functional role of MEKK 2 , MEKK 3 , and MEK 5 PB1 domains in the ERK 5 activation pathway . ^^^ The PB 1 domains of MEKK 2 and MEKK 3 bind the PB 1 domain of MEK 5 but do not significantly homo or heterodimerize with one another in vitro . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| Inhibition of ERK 5 , MEK 5 activation or activation of MEKK 2 deficient mast cells was associated with inhibition of MEF2C phosphorylation and a decrease in c Jun expression . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| MEK 5 and ERK 5 are localized in the nuclei of resting as well as stimulated cells , while MEKK 2 translocates from the cytosol to the nucleus upon stimulation . ^^^ Unlike ERK 5 and MEK 5 , their upstream activator MEKK 2 is localized mainly in the cytosol of resting cells , and translocates into the nucleus upon EGF stimulation , allowing transmission of signals to the nuclear MEK 5 . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| Certain mutations in the ERK 5 docking site that prevent MEK5 / ERK5 interaction also abrogate the ability of MEKK 2 to bind and activate MEK 5 . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| MEKK 2 , MEK 5 , and extracellular signal regulated kinase 5 ( ERK 5 ) are members of a three kinase cascade for the activation of ERK 5 . ^^^ MEK 5 is the only MAP2K to express a PB 1 domain , and we have shown that it heterodimerizes with the PB 1 domain of MEKK 2 . ^^^ Here we demonstrate the MEK 5 PB1 domain is a scaffold that also binds ERK 5 , functionally forming a MEKK 2 MEK5 ERK 5 complex . ^^^ Reconstitution assays and CFP / YFP imaging ( fluorescence resonance energy transfer [ FRET ] ) measuring YFP MEKK2 / CFP MEK 5 and CFP MEK5 / YFP ERK 5 interactions define distinct MEK 5 PB1 domain binding sites for MEKK 2 and ERK 5 , with a C terminal extension of the PB 1 domain contributing to ERK 5 binding . ^^^ |
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| Interacting proteins: Q13163 and Q9Y2U5 |
Pubmed |
SVM Score :0.0 |
| NA |
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