Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Induce the Formation of Colocalizing, Conjugated Ubiquitin
AUTOR(ES)
Parkinson, Jane
FONTE
American Society for Microbiology
RESUMO
Herpes simplex virus type 1 immediate early protein ICP0 influences virus infection by inducing the degradation of specific cellular proteins via a mechanism requiring its RING finger and the ubiquitin-proteasome pathway. Many RING finger proteins, by virtue of their RING finger domain, interact with E2 ubiquitin-conjugating enzymes and act as a component of an E3 ubiquitin ligase. We have recently shown that ICP0 induces the accumulation of colocalizing, conjugated ubiquitin, suggesting that ICP0 can act as or contribute to an E3 ubiquitin ligase. In this report we demonstrate that the ICP0-related RING finger proteins encoded by other alphaherpesviruses also induce colocalizing, conjugated ubiquitin, thereby suggesting that they act by similar biochemical mechanisms.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=114941Documentos Relacionados
- Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Affect Cellular Structures and Proteins
- ICP0 Induces the Accumulation of Colocalizing Conjugated Ubiquitin
- Physical interaction between the herpes simplex virus type 1 immediate-early regulatory proteins ICP0 and ICP4.
- Phosphorylation Site Mutations Affect Herpes Simplex Virus Type 1 ICP0 Function
- Herpes Simplex Virus ICP0 Mutants Are Hypersensitive to Interferon