Protein phosphatase 5 as a negative key regulator of Raf-1 activation.
Growth factors such as the epidermal growth factor cause sequential activation of receptor tyrosine kinases, adaptor molecules and the Raf-MEK-ERK pathway. The kinetics and intensity of these signals are dependent on the balance between phosphorylation and dephosphorylation of these molecules by numerous kinases and phosphatases, respectively. Recently, protein phosphatase 5 has been characterized as a key dephosphorylation regulator of Raf-1 activation in growth factor-mediated signaling, leading to attenuation of the MEK-ERK cascade.
Shah
Bukhtiar H
BH
Section on Hormonal Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. shahb@mail.nih.gov
Catt
Kevin J
KJ
D000818:Animals; D002454:Cell Differentiation; D049109:Cell Proliferation; D066246:ErbB Receptors / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D020930:MAP Kinase Kinase Kinases / Q000502:physiology; D008954:Models, Biological; D009687:Nuclear Proteins / Q000502:physiology*; D010749:Phosphoprotein Phosphatases / Q000502:physiology*; D019908:Proto-Oncogene Proteins c-raf / Q000378:metabolism* / Q000502:physiology; D015398:Signal Transduction
D009687:Nuclear Proteins; D066246:ErbB Receptors; D019908:Proto-Oncogene Proteins c-raf; D020930:MAP Kinase Kinase Kinases; D010749:Phosphoprotein Phosphatases; C089641:protein phosphatase 5