Identifiers
mitogen-activated protein kinase kinase 2
HUGO:MAP2K2, HGNC:6842, ENTREZ:5605, GENECARDS:GC19M004090, UNIPROT:P36507
Maps_Modules
HMC:ACTIVATING_INVASION_AND_METASTASIS
EMT Senescence / EMT_REGULATORS
EMT Senescence / MITOCHONDRIA_OXIDATIVE_STRESS
References
PMID:7565670
MEK-1/2 have a proline rich domain and critical Serine residues (MEK-1 S218/222, MEK-2 unknown, S) upon which the molecules may be phosphorylated.
MEK1/2 are found in the cytoplasm of unstimulated cells.
MEK-1/2 bind to active Raf-1 via the proline-rich domain.
Active Raf-1 is able to phosphorylate target Serine and Threonine residues in the presence of ATP
Active Raf-1 phosphorylates MEK-1/2 on Serine residues, converting ATP to ADP. The MEK-1/2 kinase is now active.
References
em_emtc_emtc_re389( EMT Senescence ):
PMID:7565670
Active Raf-1 phosphorylates MEK-1/2 on Serine residues, converting ATP to ADP. The MEK-1/2 kinase is now active.
References
em_emtc_emtc_re389( EMT Senescence ):
PMID:7565670
Active Raf-1 phosphorylates MEK-1/2 on Serine residues, converting ATP to ADP. The MEK-1/2 kinase is now active.
em_emtc_emtc_re391( EMT Senescence ):
PMID:8388392
PMID:8226933
In the cytoplasm activated MEK1 (Serine phosphorylated) may encounter monomeric, inactive ERK1.
ERK1 in its inactive form is not phosphorylated on a critical Threonine (T) and a critical Tyrosine (Y).
MEK1 phosphorylates the critical Tyr and Thr on ERK1, converting two ATP to ADP. Phosphorylation of ERK-1 activates its kinase activity.