Mechanisms of cell transformation by papillomavirus E5 proteins

被引：129

作者：

DiMaio, D ^{[1
]}

Mattoon, D ^{[1
]}

机构：

[1] Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA

来源：

ONCOGENE | 2001年 / 20卷 / 54期

关键词：

E5; protein; growth factor receptor; transmembrane protein; V-ATPase; viral oncogene;

D O I：

10.1038/sj.onc.1204915

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The papillomavirus E5 proteins are short, hydrophobic transforming proteins. The transmembrane E5 protein encoded by bovine papillomavirus transforms cells by activating the platelet-derived growth factor beta receptor tyrosine kinase in a ligand-independent fashion. The bovine papillomavirus E5 protein forms a stable complex with the receptor, thereby inducing receptor dimerization and activation, trans-phosphorylation, and recruitment of cellular signaling proteins to the receptor. The E5 proteins of the human papillomaviruses also appear to affect the activity of growth factor receptors and their signaling pathways. The interaction of papillomavirus E5 proteins with a subunit of the vacuolar ATPase may also contribute to transformation. Further analysis of these unique mechanisms of viral transformation will yield new insight into the regulation of growth factor receptor activity and cellular signal transduction pathways.

引用

页码：7866 / 7873

页数：8

共 73 条

[1] A mutagenic analysis of the E5 protein of human papillomavirus type 16 reveals that E5 binding to the vacuolar H+-ATPase is not sufficient for biological activity, using mammalian and yeast expression systems [J].

Adam, JL ;

Briggs, MW ;

McCance, DJ .

VIROLOGY, 2000, 272 (02) :315-325

[2] The transmembrane domain of the E5 oncoprotein contains functionally discrete helical faces [J].

Adduci, AJ ;

Schlegel, R .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (15) :10249-10258

[3] VACUOLAR H+-ATPASE MUTANTS TRANSFORM CELLS AND DEFINE A BINDING-SITE FOR THE PAPILLOMAVIRUS E5 ONCOPROTEIN [J].

ANDRESSON, T ;

SPARKOWSKI, J ;

GOLDSTEIN, DJ ;

SCHLEGEL, R .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (12) :6830-6837

[4] Cooperative transformation and coexpression of bovine papillomavirus type 1 E5 and E7 proteins [J].

Bohl, J ;

Hull, B ;

Vande Pol, SB .

JOURNAL OF VIROLOGY, 2001, 75 (01) :513-521

[5] THE HUMAN PAPILLOMAVIRUS TYPE-16 E5 GENE COOPERATES WITH THE E7 GENE TO STIMULATE PROLIFERATION OF PRIMARY-CELLS AND INCREASES VIRAL GENE-EXPRESSION [J].

BOUVARD, V ;

MATLASHEWSKI, G ;

GU, ZM ;

STOREY, A ;

BANKS, L .

VIROLOGY, 1994, 203 (01) :73-80

[6] The human papillomavirus type 16 E5 protein alters vacuolar H+-ATPase function and stability in Saccharomyces cerevisiae [J].

Briggs, MW ;

Adam, JL ;

McCance, DJ .

VIROLOGY, 2001, 280 (02) :169-175

[7] THE E5-ONCOPROTEIN OF BOVINE PAPILLOMAVIRUS IS ORIENTED ASYMMETRICALLY IN GOLGI AND PLASMA-MEMBRANES [J].

BURKHARDT, A ;

WILLINGHAM, M ;

GAY, C ;

JEANG, KT ;

SCHLEGEL, R .

VIROLOGY, 1989, 170 (01) :334-339

[8] LOCALIZATION OF BOVINE PAPILLOMAVIRUS TYPE-1 E5 PROTEIN TO TRANSFORMED BASAL KERATINOCYTES AND PERMISSIVE DIFFERENTIATED CELLS IN FIBROPAPILLOMA TISSUE [J].

BURNETT, S ;

JAREBORG, N ;

DIMAIO, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (12) :5665-5669

[9] Mutational analysis of human papillomavirus type 11 E5a oncoprotein [J].

Chen, SL ;

Tsai, TC ;

Han, CP ;

Tsao, YP .

JOURNAL OF VIROLOGY, 1996, 70 (06) :3502-3508

[10] TRANSFORMING ACTIVITY OF E5A PROTEIN OF HUMAN PAPILLOMAVIRUS TYPE-6 IN NIH-3T3 AND C127 CELLS [J].

CHEN, SL ;

MOUNTS, P .

JOURNAL OF VIROLOGY, 1990, 64 (07) :3226-3233

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