|
|
|
|
|
|
|
|
|
|
Expert Reviews in Molecular Medicine: http://www.expertreviews.org/
Accession information: (02)00439-8h.htm (shortcode: fig001wkg); 25 April 2002
Reprint/PDF version Back
to main article
Schematic representation of the structure and phosphorylation of Raf-1
Walter Kolch, Ashwin
Kotwaliwale, Keith Vass and Petra Janosch
Author
contact details
Figure 1. Schematic representation of the structure and phosphorylation of Raf-1. The three conserved regions (CR1–3) are shown: CR1 has a Ras-binding domain and a Cys-rich domain; CR2 is a Ser/Thr-rich domain; CR3 is required for kinase activity. The dotted line in CR1 indicates that the Cys-rich domain is not essential for Ras binding but is required for activation of Raf by Ras. Several kinases, including PAK (p21rac/cdc42-activated kinase), Src-family tyrosine kinases and as yet undefined kinases, phosphorylate Raf-1. Ser338 can be phosphorylated by PAK, and Tyr341 by Src. The phosphorylation sites (P) and their functions (when phosphorylated) are indicated. MEK, MAPK/ERK kinase (fig001wkg).
|
home | search
| glossary
| links
| sitemap | contact
|
Expert Reviews in
Molecular Medicine © Cambridge University
Press ISSN 1462-3994 (Disclaimer
and copyright)
Editorial Office: Centre for Applied Research
in Educational Technologies (CARET), 1st Floor, 16 Mill Lane, Cambridge,
CB2 1SB, UK. Tel: +44 (0)1223 765 375; Fax: +44(0)1223 765 505; E-mail: ermm@caret.cam.ac.uk