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  • 1
    Keywords: EXPRESSION ; Germany ; IN-VIVO ; PATHWAY ; PATHWAYS ; VIVO ; PROTEIN ; FAMILY ; DOMAIN ; BINDING ; ASSAY ; PLASMA ; PLASMA-MEMBRANE ; DEGRADATION ; INVOLVEMENT ; KINASE-C ; DOMAINS ; INTERCELLULAR COMMUNICATION ; CARDIAC MYOCYTES ; ASSAYS ; in vivo ; PROLINE ; JUNCTION ; connexin ; EPITHELIAL NA+ CHANNEL ; GAMMA-ENAC ; gap junction ; GAP-JUNCTION PROTEIN ; PY motif ; ubiquitylation ; WW DOMAINS
    Abstract: Connexin43 is degraded by the proteasomal as well as the lysosomal pathway with ubiquitin playing a role in both degradation pathways. So far, no ubiquitin protein ligase has been identified for any of the connexins. By using pull-down assays, here we show binding of a ubiquitin protein ligase, Nedd4, to the C-terminus of connexin43. This observation was confirmed in vivo by coimmunoprecipitation and immunofluorescence, showing colocalization of Nedd4 and connexin43. Binding of Nedd4 to its interaction partners is generally carried out by its WW domains. Our results indicate that the interaction with connexin43 occurs through all three WW domains of Nedd4. Furthermore, whereas WW1 and WW2 domains mainly interact with the unphosphorylated form of connexin43, WW3 binds phosphorylated and unphosphorylated forms equally. In addition, using the surface plasmon resonance approach we show that only the WW2 domain binds to the PY motif located at the C-terminus of connexin43. Suppression of Nedd4 expression with siRNA resulted in an accumulation of gap junction plaques at the plasma membrane, suggesting an involvement of the ubiquitin protein ligase Nedd4 in gap junction internalization
    Type of Publication: Journal article published
    PubMed ID: 16931598
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  • 2
    Keywords: APOPTOSIS ; CANCER ; CELLS ; EXPRESSION ; proliferation ; CELL ; Germany ; human ; INFORMATION ; GENE ; GENOME ; PROTEIN ; PROTEINS ; transcription ; DIFFERENTIATION ; TISSUE ; MICE ; DNA ; TISSUES ; SKIN ; BINDING ; BIOLOGY ; MOLECULAR-BIOLOGY ; papillomavirus ; TARGET ; virus ; NO ; TRANSGENIC MICE ; PROMOTER ; PROMOTERS ; cervical cancer ; CERVICAL-CANCER ; REGION ; human papillomavirus ; HIGH-RISK ; HPV ; transactivation ; ONCOGENE ; HUMAN-PAPILLOMAVIRUS ; CERVICAL-CARCINOMA ; NETHERLANDS ; REPRESSION ; molecular biology ; molecular ; RE ; PATTERN ; LEVEL ; analysis ; methods ; EVENTS ; LOSSES ; UBIQUITIN ; CANCERS ; microbiology ; E2 PROTEIN ; HUMAN PAPILLOMAVIRUSES ; animal model ; host ; viral ; UPSTREAM ; UBIQUITIN-C ; biotechnology ; E2 ; READING FRAMES ; E6 PROMOTER ; PAPILLOMAVIRUS DNA-REPLICATION ; ubiquitin C promoter
    Abstract: The E2 early protein of human papillomaviruses (HPV) has been found associated with the mitotic spindle therefore being implicated in the partition of the replicated viral DNA to daughter cells. In addition, E2 proteins bind to the upstream regulatory region of the virus and to cellular promoters modulating thereby cellular transcription and differentiation. In many cervical cancers, the E2 reading frame is interrupted upon incorporation of the viral genome into the host DNA. This results in the loss of the E2 mediated transcriptional repression and uncontrolled expression of the viral oncogenes. All these results have been obtained in transfected cells but no information is available on the E2 effects in the context of the entire organism. Transgenic mice were generated expressing the E2 protein of HPV11 under the control of the Ubiquitin C promoter. E2 mRNA is present in all mice tissues analysed and the E2 protein expressed in the skin (the target tissue of HPV11) was shown by Western blotting, albeit at a very low level. Analysis of the transgenic mice shows no major histological changes in the skin or all other tissues investigated. These data indicate that in transgenic mice the human papillomavirus type 11 E2 does not grossly modulate cellular proliferation or differentiation events
    Type of Publication: Journal article published
    PubMed ID: 17701441
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