Raf-1: A kinase currently without a cause but not lacking in effects

The protein product of the c-raf-1 gene, designated Raf-1, is a 70-75 kd phosphoprotein with intrinsic kinase activity toward serine and threonine residues. Sequence analysis of the protein suggests a two-domain structure, with a kinase domain occupying the carboxy-terminal half of the molecule and...

Full description

Saved in:
Bibliographic Details
Published inCell Vol. 64; no. 3; pp. 479 - 482
Main Authors Li, Ping, Wood, Kenneth, Mamon, Harvey, Haser, Wayne, Roberts, Tom
Format Book Review Journal Article
LanguageEnglish
Published Cambridge, MA Elsevier Inc 08.02.1991
Cell Press
Subjects
Online AccessGet full text
ISSN0092-8674
DOI10.1016/0092-8674(91)90228-Q

Cover

Loading…
More Information
Summary:The protein product of the c-raf-1 gene, designated Raf-1, is a 70-75 kd phosphoprotein with intrinsic kinase activity toward serine and threonine residues. Sequence analysis of the protein suggests a two-domain structure, with a kinase domain occupying the carboxy-terminal half of the molecule and a potential regulatory domain making up the remainder. A variety of biochemical experiments show that the Raf-1 molecule behaves in a manner consistent with its proposed role as a signal transducer for tyrosine kinases. Antibodies against the Ras protein were able to block the action not only of Ras itself but of tyrosine kinases. Notably, the activities of both v-Raf and v-Mos, a more distant member of the Raf family, were not subject to interference by the anti-Ras antibodies. This suggests either that Raf-1 acts downstream of both Ras and tyrosine kinases or that Raf-1 acts through an independent mechanism.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ObjectType-Article-1
ObjectType-Feature-2
ObjectType-Review-3
ISSN:0092-8674
DOI:10.1016/0092-8674(91)90228-Q