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HPV E6 and MAGUK protein interactions: determination of the molecular basis for specific protein recognition and degradation.

Abstract：

:It has recently been shown that the high-risk human papillomavirus (HPV) E6 proteins can target the PDZ-domain containing proteins, Dlg, MUPP-1, MAGI-1 and hScrib for proteasome-mediated degradation. However, the E6 proteins from HPV-16 and HPV-18 (the two most common high-risk virus types) differ in their ability to target these proteins in a manner that correlates with their malignant potential. To investigate the underlying mechanisms for this, we have mutated HPV-16 and HPV-18 E6s to give each protein the other's PDZ-binding motif. Analysis of these mutants shows that the greater ability of HPV-18 E6 to bind to these proteins and to target them for degradation is indeed due to a single amino acid difference. Using a number of assays, we show that the E6 proteins interact specifically with only one of the five PDZ domains of MAGI-1, and this is the first interaction described for this particular PDZ domain. We also show that the guanylate kinase homology domain and the regions of MAGI-1 downstream of amino acid 733 are not required for the degradation of MAGI-1. Finally, in a series of comparative analyses, we show that the degradation of MAGI-1 occurs through a different mechanism from that used by the E6 protein to induce the degradation of Dlg and p53.

journal_name

Oncogene

journal_title

Oncogene

authors

Thomas M,Glaunsinger B,Pim D,Javier R,Banks L

doi

10.1038/sj.onc.1204719

subject

Has Abstract

pub_date

2001-09-06 00:00:00

pages

5431-9

issue

39

eissn

0950-9232

issn

1476-5594

journal_volume

20

pub_type

杂志文章

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