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Sci. STKE, 22 February 2000
Vol. 2000, Issue 20, p. tw6
[DOI: 10.1126/stke.2000.20.tw6]

EDITORS' CHOICE

Ras Ras Dimers in the Membrane

Membrane localization of the small GTP-binding protein Ras is essential for its function. Upon activation, Ras binds to the serine-threonine kinase Raf-1. Inouye et al. suggest that Ras must dimerize at the membrane to activate Raf-1. Purified, GTP-bound Ras that was incorporated into liposomes formed dimers that activated Raf-1 in the absence of other membrane proteins. This effect did not occur in the absence of liposomes. Ras fusion proteins that formed dimers could bypass incorporation into liposomes for Raf-1 activation, and Ras fusion proteins induced to dimerize in intact cells also activated Raf-1. It remains unclear how Ras might dimerize in the membrane.

Inouye, K., Mizutani, S., Koide, H., and Kaziro, Y. (2000) Formation of the Ras dimer is essential for Raf-1 activation. J. Biol. Chem. 275: 3737-3740. [Abstract] [Full Text]

Citation: Ras Dimers in the Membrane. Sci. STKE 2000, tw6 (2000).


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