Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains-Reference-Cited by-同舟云学术

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Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains

Published:1999-05-15 Issue:2 Volume:1 Page:98-105
ISSN:1465-7392
Container-title:Nature Cell Biology
language:en
Short-container-title:Nat Cell Biol

Author:

Roy Sandrine,Luetterforst Robert,Harding Angus,Apolloni Ann,Etheridge Maria,Stang Espen,Rolls Barbara,Hancock John F.,Parton Robert G.

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology

Link

http://www.nature.com/articles/ncb0699_98.pdf

Reference50 articles.

1. Hancock, J. F., Magee, A. I., Childs, J. E. & Marshall, C. J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167–1177 ( 1989).

2. Hancock, J. F., Paterson, H. & Marshall, C. J. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63, 133–139 ( 1990).

3. Resh, M. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76, 411–413 ( 1994).

4. Wedegaertner, P. B., Wilson, P.T. & Bourne, H. R. Lipid modifications of trimeric G proteins. J. Biol. Chem. 270, 503–506 (1995).

5. Umanoff, H., Edelmann, W., Pellicer, A. & Kucherlapati, R. The murine N-Ras gene is not essential for growth and development. Proc. Natl Acad. Sci. USA 92, 1709– 1713 (1995).

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