Published February 2014 | Version v1
Journal article

The human papillomavirus (HPV) E6 oncoproteins promotes nuclear localization of active caspase 8

  • 1. Unidad de Investigación Biomédica en Cáncer, Instituto Nacional de Cancerología, México/Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México. Av. San Fernando No. 22, Col. Sección XVI, Tlalpan 14080 (Mexico)
  • 2. International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34149 Trieste (Italy)

Description

The HPV-16 E6 and E6 proteins have been shown previously to be capable of regulating caspase 8 activity. We now show that the capacity of E6 to interact with caspase 8 is common to diverse HPV types, being also seen with HPV-11 E6, HPV-18 E6 and HPV-18 E6. Unlike most E6-interacting partners, caspase 8 does not appear to be a major proteasomal target of E6, but instead E6 appears able to stimulate caspase 8 activation, without affecting the overall apoptotic activity. This would appear to be mediated in part by the ability of the HPV E6 oncoproteins to recruit active caspase 8 to the nucleus. - Highlights: • Multiple HPV E6 oncoproteins interact with the caspase 8 DED domain. • HPV E6 stimulates activation of caspase 8. • HPV E6 promotes nuclear accumulation of caspase 8

Availability note (English)

Available from http://dx.doi.org/10.1016/j.virol.2013.12.013

Additional details

Identifiers

DOI
10.1016/j.virol.2013.12.013;
PII
S0042-6822(13)00676-4;

Publishing Information

Journal Title
Virology
Journal Volume
450-451
Journal Page Range
p. 146-152
ISSN
0042-6822
CODEN
VIRLAX

INIS

Country of Publication
United States
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
47004456
Subject category
S60: APPLIED LIFE SCIENCES;
Descriptors DEI
APOPTOSIS; CELL NUCLEI; ENZYMES; HUMAN POPULATIONS; ONCOGENIC VIRUSES
Descriptors DEC
CELL CONSTITUENTS; MICROORGANISMS; ORGANIC COMPOUNDS; PARASITES; POPULATIONS; PROTEINS; VIRUSES

Optional Information

Copyright
Copyright (c) 2013 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.