Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein.
Human papillomaviruses (HPVs) are associated with the majority of cervical cancers and encode a transforming protein, E6, that interacts with the tumor suppressor protein p53. Because E6 has p53-independent transforming activity, the yeast two-hybrid system was used to search for other E6-binding proteins. One such protein, E6BP, interacted with cancer-associated HPV E6 and with bovine papillomavirus type 1 (BPV-1) E6. The transforming activity of BPV-1 E6 mutants correlated with their E6BP-binding ability. E6BP is identical to a putative calcium-binding protein, ERC-55, that appears to be localized in the endoplasmic reticulum.
Chen
J J
JJ
Department of Dermatology, New England Medical Center, Boston, MA, USA.
Reid
C E
CE
Band
V
V
Androphy
E J
EJ
D052688:Bovine papillomavirus 1 / Q000502:physiology; D002135:Calcium-Binding Proteins / Q000032:analysis / Q000378:metabolism*; D002472:Cell Transformation, Viral; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000737:chemistry; D006367:HeLa Cells; D006801:Humans; D009856:Oncogene Proteins, Viral / Q000032:analysis / Q000378:metabolism*; D027383:Papillomaviridae; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012097:Repressor Proteins; D044767:Ubiquitin-Protein Ligases; D014764:Viral Proteins / Q000378:metabolism
D002135:Calcium-Binding Proteins; C068651:E6 protein, Human papillomavirus type 16; D009856:Oncogene Proteins, Viral; C088393:RCN2 protein, human; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; D014764:Viral Proteins; C059269:protein E6, Bovine papillomavirus; D044767:Ubiquitin-Protein Ligases