Publication Date:
1995-07-28
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J J -- Reid, C E -- Band, V -- Androphy, E J -- R01CA44174/CA/NCI NIH HHS/ -- R29CA56803/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):529-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, New England Medical Center, Boston, MA, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624774" target="_blank"〉PubMed〈/a〉
Keywords:
Bovine papillomavirus 1/physiology
;
Calcium-Binding Proteins/analysis/*metabolism
;
Cell Transformation, Viral
;
Cells, Cultured
;
Endoplasmic Reticulum/chemistry
;
HeLa Cells
;
Humans
;
Oncogene Proteins, Viral/analysis/*metabolism
;
*Papillomaviridae
;
Recombinant Fusion Proteins/metabolism
;
*Repressor Proteins
;
Ubiquitin-Protein Ligases
;
Viral Proteins/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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