K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes.

@article{Silvius2006Kras4BAP,
  title={K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes.},
  author={John R Silvius and Pinkesh Bhagatji and Rania Leventis and Donato Terrone},
  journal={Molecular biology of the cell},
  year={2006},
  volume={17 1},
  pages={
          192-202
        }
}
We have used fluorescence microscopy and the technique of rapamycin-regulated protein heterodimerization to examine the dynamics of the subcellular localizations of fluorescent proteins fused to lipid-modified protein sequences and to wild-type and mutated forms of full-length K-ras4B. Singly prenylated or myristoylated fluorescent protein derivatives lacking a "second signal" to direct them to specific subcellular destinations, but incorporating a rapamycin-dependent heterodimerization module… CONTINUE READING

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