BOVINE PAPILLOMAVIRUS-E5 ONCOPROTEIN BINDS TO THE 16K COMPONENT OF VACUOLAR H+-ATPASES

被引：171

作者：

GOLDSTEIN, DJ ^{[1
]}

FINBOW, ME ^{[1
]}

ANDRESSON, T ^{[1
]}

MCLEAN, P ^{[1
]}

SMITH, K ^{[1
]}

BUBB, V ^{[1
]}

SCHLEGEL, R ^{[1
]}

机构：

[1] BEATSON INST CANC RES,GLASGOW G61 1BD,SCOTLAND

来源：

NATURE | 1991年 / 352卷 / 6333期

关键词：

D O I：

10.1038/352347a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

THE major transforming protein of bovine papillomavirus type 1, E5 (refs 1-4), is mainly associated with endomembranes 5,6, specifically binding to a cellular protein of relative molecular mass 16,000 (16K) (ref. 7). At the same time as transformation, E5 causes the phosphorylation of tyrosine residues in epidermal and platelet-derived growth factor receptors 8,9. We show here that the 16K protein associated with E5 is the 16K component of vacuolar ATPases. This protein is known to be an integral membrane protein in endosomes, bovine chromaffin granules, synaptic vesicles, fungal and plant vacuoles and clathrin-coated vesicles 10-16, as well as a component of gap-junction-like membrane complexes 17. Because proton pumps are critical for the function of cellular compartments that process growth-factor receptors, the interaction of E5 with the 16K protein could explain the pleiomorphic features of cells transformed by E5.

引用

页码：347 / 349

页数：3

共 26 条

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