Increased tyrosine kinase activity associated with the protein encoded by the activated neu oncogene.

Abstract:

:A single mutation altering the transmembrane domain of the receptor-like p185 protein encoded by the rat neu gene converts the normal neu gene into a potent oncogene. The biochemical consequences of this mutation were studied by examining phosphorylation of the normal and transforming p185 molecules in membrane preparations. Here we show that the transforming p185 is phosphorylated to a much higher extent in vitro than its normal counterpart. This preferential phosphorylation has the properties that would be expected of p185 autophosphorylation: it takes place on tyrosine and requires intact p185 kinase activity. The normal p185 protein does not demonstrate increased phosphorylation even when it coexists in a transformed cell with the transforming p185 protein. These data show that transforming p185 is specifically associated with an active tyrosine kinase activity and suggest that this activity is intrinsic to the transforming protein. Thus, the transmembrane domain of p185 appears to directly regulate its kinase activity.

authors

Bargmann CI,Weinberg RA

doi

10.1073/pnas.85.15.5394

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

5394-8

issue

15

eissn

0027-8424

issn

1091-6490

journal_volume

85

pub_type

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