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Ras hitchhikes on PDE6δ

Nature Cell Biology volume 14, pages 128–129 (2012)Cite this article

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Ras GTPases are tethered to cellular membranes by a farnesyl lipid that modifies a carboxy-terminal cysteine. One of the ways Ras traffics between membranes is via fluid-phase diffusion, suggesting that a cytosolic chaperone might be needed to shield the farnesyl lipid during transport. PDE6δ is now revealed to be a farnesyl-binding chaperone that facilitates the trafficking and signalling of Ras.

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Figure 1: PDE6δ is a Ras chaperone that facilitates cytoplasmic trafficking.

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  1. Mark R. Philips is at the NYU Cancer Institute, 522 First Avenue, New York, New York 10016, USA,

    Mark R. Philips

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  1. Mark R. Philips
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Correspondence to Mark R. Philips.

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Philips, M. Ras hitchhikes on PDE6δ. Nat Cell Biol 14, 128–129 (2012). https://doi.org/10.1038/ncb2429

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