Ubiquitin-proteasome-dependent slingshot 1 downregulation in neuronal cells inactivates cofilin to facilitate HSV-1 replication

Virology. 2014 Jan 20:449:88-95. doi: 10.1016/j.virol.2013.11.011. Epub 2013 Nov 26.

Abstract

Actin and its regulators are critical for neuronal function. Infection with herpes simplex virus 1 (HSV-1) remodels neuronal cell actin dynamics, which may relate virus-induced pathological processes in the nervous system. We previously demonstrated that cofilin is an actin regulator that participates in HSV-1-induced actin dynamics in neuronal cells, but how HSV-1 regulates cofilin has remained unclear. In the present study, we demonstrated the HSV-1-induced the inactivation of cofilin and the accumulation of phosphorylated cofilin in the nucleus, which together benefited viral replication. This consistent cofilin inactivation was achieved by the downregulation of slingshot 1 (SSH1). Notably, virus-induced SSH1 downregulation depended on the ubiquitin-proteasome system. Cofilin inactivation is therefore critical for HSV-1 replication during neuronal infection and is maintained by SSH1 downregulation. Moreover, these results provide new insight into the HSV-1-induced neurological pathogenesis and suggest potential new strategies to inhibit HSV-1 replication.

Keywords: Cofilin; F-actin; HSV-1; LIM kinase-1; LIMK1; SSH1; Ubiquitin-proteasome; actin filaments; herpes simplex virus 1; p-cofilin; phosphorylated cofilin; slingshot-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism
  • Cofilin 1 / genetics
  • Cofilin 1 / metabolism*
  • Down-Regulation
  • Herpes Simplex / enzymology*
  • Herpes Simplex / genetics
  • Herpes Simplex / virology
  • Herpesvirus 1, Human / genetics
  • Herpesvirus 1, Human / physiology*
  • Humans
  • Neurons / metabolism
  • Neurons / virology*
  • Phosphoprotein Phosphatases
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Transport
  • Ubiquitin / metabolism*
  • Virus Replication*

Substances

  • Cofilin 1
  • Ubiquitin
  • Phosphoprotein Phosphatases
  • SSH1 protein, human
  • Proteasome Endopeptidase Complex