Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1.
In higher eukaryotes, the Ras and Raf-1 proto-oncoproteins transduce growth and differentiation signals initiated by tyrosine kinases. The Ras polypeptide and the amino-terminal regulatory domain of Raf-1 (residues 1-257) are shown to interact, directly in vitro and in a yeast expression system. Raf-1 (1-257) binds GTP-Ras in preference to GDP-Ras, and inhibits Ras-GAP activity. Mutations in and around the Ras effector domain impair Ras binding to Raf-1 (1-257) and Ras transforming activity in parallel.
Zhang
X F
XF
Diabetes Unit, Harvard Medical School, Charlestown, Massachusetts.
Settleman
J
J
Kyriakis
J M
JM
Takeuchi-Suzuki
E
E
Elledge
S J
SJ
Marshall
M S
MS
Bruder
J T
JT
Rapp
U R
UR
Avruch
J
J
D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001665:Binding Sites; D002478:Cells, Cultured; D005822:Genetic Vectors; D009036:Moths; D009154:Mutation; D015689:Oncogene Protein p21(ras) / Q000378:metabolism*; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D019908:Proto-Oncogene Proteins c-raf; D016283:Proto-Oncogene Proteins p21(ras) / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D015398:Signal Transduction / Q000502:physiology
D011518:Proto-Oncogene Proteins; D011993:Recombinant Fusion Proteins; D017346:Protein Serine-Threonine Kinases; D019908:Proto-Oncogene Proteins c-raf; D015689:Oncogene Protein p21(ras); D016283:Proto-Oncogene Proteins p21(ras)