IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Human and primate tumour viruses use PDZ binding as an evolutionarily conserved mechanism of targeting cell polarity regulators.
Autor/es:
TOMAIC V, GARDIOL D, MASSIMI P, OZBUM M, MYER M AND BANKS L
Revista:
ONCOGENE
Editorial:
Nature Publishing Group
Referencias:
Año: 2009 vol. 28 p. 1 - 8
ISSN:
0950-9232
Resumen:
A unique feature of the cancer-causing mucosotropic
human papillomaviruses (HPVs) is the ability of their E6
proteins to interact with a number of PDZ domaincontaining
cellular substrates, including the cell polarity
regulators hDlg and hScrib. These interactions are
essential for the ability of these viruses to induce
malignant progression. Rhesus papillomaviruses (RhPV)
are similar to their human counterparts in that they also
cause anogenital malignancy in their host, the Rhesus
Macaque. However, unlike HPV E6, the RhPV E6 has no
PDZ-binding motif. We now show that such a motif is
present on the RhPV E7 oncoprotein. This motif
specifically confers PDZ-binding activity and directs the
interaction of RhPV E7 with the cell polarity regulator
Par3, which it targets for proteasome-mediated degradation.
These results demonstrate an amazing evolutionary
conservation of function between the RhPV and the HPV
oncoproteins, where both target proteins of the same cell
polarity control network, although through different
components and pathways.