Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-1-22
pubmed:abstractText
The E2 protein of the papillomavirus plays an essential role in the viral life cycle. Through a yeast two-hybrid screening, human polo-like kinase 1 was found to interact with human papillomavirus type 5 E2. Further characterization identified that the domains responsible for the interaction are the transactivation domain of HPV-5 E2 and the sequence between the kinase and the polo box domains of Plk1. In vivo, Plk1 and HPV-5 E2 are colocalized at the nuclear speckles. In the skin epithelium not infected with epidermodysplasia verruciformis associated HPVs, Plk1 is expressed in the stratum basale, indicating that the Plk1-HPV-5 E2 interaction likely occurs in the keratinocytes at the basal layer of the epithelium upon infection of HPV-5. Both HPV-5 E2 and Plk1 also interact with the E2 binding domain of Brd4. The E2 binding domain of Brd4 is phosphorylated by Plk1 in vitro, and this phosphorylation event is blocked by the presence of HPV-5 E2. Hence, these findings suggest the possibility that the cellular function of Brd4 is de-regulated by forming a complex with HPV-5 E2 in the infected epithelial cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1096-9071
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
536-44
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Interaction between human papillomavirus type 5 E2 and polo-like kinase 1.
pubmed:affiliation
Department of Life Science, Institute of Molecular Biology, National Chung Cheng University, Chiayi, Taiwan ROC.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't