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...
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Published in | Cell Vol. 64; no. 3; pp. 479 - 482 |
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Main Authors | , , , , |
Format | Book Review Journal Article |
Language | English |
Published |
Cambridge, MA
Elsevier Inc
08.02.1991
Cell Press |
Subjects | |
Online Access | Get full text |
ISSN | 0092-8674 |
DOI | 10.1016/0092-8674(91)90228-Q |
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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. |
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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 |