Vietnam’s political economy: a discussion on the 1986-2016 period

Being a member of the thriving ASEAN and successfully implementing economic renovation (Doi Moi) have drawn the world's attention on Vietnam around the turn of the millennium. Some even expected a much faster pace of transformation, and renewed economic, AND political, reforms in Vietnam, or Doi Moi II.However, in the recent transition turmoil the Vietnamese economy has experienced some significant setback, and the solution for getting the country out of the downward spiral of low productivity, waning purchasing power and increasing costs of doing business cannot be worked out without addressing those political economy issues that have shaped the modus operandi of the nation's economic system. This article discusses the post-Doi Moi political economy in Vietnam, from 1986 to 2016 – when the 12th Congress of the Communist Party of Vietnam takes place – and prospects of reviving reform momentum in subsequent years.

ERM transactivation is up-regulated by the repression of DNA binding after the PKA phosphorylation of a consensus site at the edge of the ETS domain

The final step of the transduction pathway is the activation of gene transcription, which is driven by kinase cascades leading to changes in the activity of many transcription factors. Among these latter, PEA3/E1AF, ER81/ETV1, and ERM, members of the well conserved PEA3 group from the Ets family are involved in these processes. We show here that protein kinase A (PKA) increases the transcriptional activity of human ERM and human ETV1, through a Ser residue situated at the edge of the ETS DNA-binding domain. PKA phosphorylation does not directly affect the ERM transactivation domains but does affect DNA binding activity. Unphosphorylated wild-type ERM bound DNA avidly, whereas after PKA phosphorylation it did so very weakly. Interestingly, S367A mutation significantly reduced the ERM-mediated transcription in the presence of the kinase, and the DNA binding of this mutant, although similar to that of unphosphorylated wild-type protein, was insensitive to PKA treatment. Mutations, which may mimic a phosphorylated serine, converted ERM from an efficient DNA-binding protein to a poor DNA binding one, with inefficiency of PKA phosphorylation. The present data clearly demonstrate a close correlation between the capacity of PKA to increase the transactivation of ERM and the drastic down-regulation of the binding of the ETS domain to the targeted DNA. What we thus demonstrate here is a relatively rare transcription activation mechanism through a decrease in DNA binding, probably by the shift of a non-active form of an Ets protein to a PKA-phosphorylated active one, which should be in a conformation permitting a transactivation domain to be active.