Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline . A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
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SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (MAPKK-activated)
Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC 2.7.12.2, mitogen-activated protein kinase kinase (MAPKK) is necessary for enzyme activation. Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline [6]. A distinguishing feature of all MAPKs is the conserved sequence Thr-Xaa-Tyr (TXY). Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation. Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumour necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischaemic injury.
ceramide activation of mitochondrial p38 mitogen-activated protein kinase is a potential mechanism for loss of mitochondrial transmembrane potential and apoptosis
p38 MAPK, ERK1, and ERK2 are involved in regulation of connective tissue growth factor, CTGF, in chondrocyte maturation and function, particularly in the hypertrophic zone, as part of the retinoid and BMP signaling pathways, overview, p38 MAPK stimulates CTGF expression, while ERK1 and ERK2 supress it
ceramide activation of mitochondrial p38 mitogen-activated protein kinase is a potential mechanism for loss of mitochondrial transmembrane potential and apoptosis
p38 MAPK, ERK1, and ERK2 are involved in regulation of connective tissue growth factor, CTGF, in chondrocyte maturation and function, particularly in the hypertrophic zone, as part of the retinoid and BMP signaling pathways, overview, p38 MAPK stimulates CTGF expression, while ERK1 and ERK2 supress it
selective to p38 MAPKalpha and -beta isoforms, enhances strain-induced ERK1/2 activation but also restricts strain-induced ERK1/2 activation at longer times
selective to p38 MAPKalpha and -beta isoforms, addition to AS cells reveals marked reduction in coat size, both basal and strain-induced hyaluronan release is significantly reduced, enhances strain-induced ERK1/2 activation but also restricts strain-induced ERK1/2 activation at longer times
inhibition of the MEK-ERK pathway by either U0126 or PD98059 has no discernable effect on p38 MAPK phosphorylation, U0126 treatment also fails to modify pervanadate-induced p38 MAPK activity
mechanical strain activates ERK but not p38 MAPK. ERK1/2, but not p38 MAPK, exhibits dose-dependent FGF2-, epidermal growth factor- or sodium pervanadate-induced activation
constitutively active p38 MAPK serves an essential, permissive role in mechanically induced changes in ERK activation and in the accumulation of hyaluronan-rich extracellular matrices that serve a key role in joint development, constitutively active p38 influences the duration and extent of ERK1/2 activation and hyperphosphorylation of one of its downstream targets c-Fos
Ceramide activates a mitochondrial p38 mitogen-activated protein kinase: a potential mechanism for loss of mitochondrial transmembrane potential and apoptosis