title: Interaction between human papillomavirus type 5 E2 and polo-like kinase 1.
abstract: 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.
authors.affiliation: Department of Life Science, Institute of Molecular Biology, National Chung Cheng University, Chiayi, Taiwan ROC.
authors.forename: Wei-Sheng
authors.initials: WS
authors.lastname: Wang
authors.forename: Moon-Sing
authors.initials: MS
authors.lastname: Lee
authors.forename: Chih-En
authors.initials: CE
authors.lastname: Tseng
authors.forename: I-Huan
authors.initials: IH
authors.lastname: Liao
authors.forename: Shu-Ping
authors.initials: SP
authors.lastname: Huang
authors.forename: Ru-Inn
authors.initials: RI
authors.lastname: Lin
authors.forename: Chin
authors.initials: C
authors.lastname: Li
mesh_terms: D018797:Cell Cycle Proteins / Q000378:metabolism*; D002460:Cell Line; D002467:Cell Nucleus / Q000737:chemistry; D006801:Humans; D015603:Keratinocytes / Q000821:virology; D009687:Nuclear Proteins / Q000378:metabolism; D027383:Papillomaviridae / Q000502:physiology*; D010766:Phosphorylation; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D014157:Transcription Factors / Q000378:metabolism; D020798:Two-Hybrid System Techniques; D017361:Viral Nonstructural Proteins / Q000378:metabolism*; D000097869:Polo-Like Kinase 1; D000092468:Bromodomain Containing Proteins
chemical_list: D018797:Cell Cycle Proteins; D009687:Nuclear Proteins; D017346:Protein Serine-Threonine Kinases; D011518:Proto-Oncogene Proteins; D014157:Transcription Factors; D017361:Viral Nonstructural Proteins; D000097869:Polo-Like Kinase 1; C441289:BRD4 protein, human; D000092468:Bromodomain Containing Proteins