The RafC1 cysteine-rich domain contains multiple distinct regulatory epitopes which control Ras-dependent Raf activation.

@article{Daub1998TheRC,
  title={The RafC1 cysteine-rich domain contains multiple distinct regulatory epitopes which control Ras-dependent Raf activation.},
  author={Michael Daub and Johannes J{\"o}ckel and Thomas Quack and Christoph K. Weber and Frank Schmitz and Ulf R{\"u}diger Rapp and Alfred Wittinghofer and Christoph Block},
  journal={Molecular and cellular biology},
  year={1998},
  volume={18 11},
  pages={6698-710}
}
Activation of c-Raf-1 (referred to as Raf) by Ras is a pivotal step in mitogenic signaling. Raf activation is initiated by binding of Ras to the regulatory N terminus of Raf. While Ras binding to residues 51 to 131 is well understood, the role of the RafC1 cysteine-rich domain comprising residues 139 to 184 has remained elusive. To resolve the function of the RafC1 domain, we have performed an exhaustive surface scanning mutagenesis. In our study, we defined a high-resolution map of multiple… CONTINUE READING