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Lipid modifications of G proteins.

Publication ,  Journal Article
Casey, PJ
Published in: Curr Opin Cell Biol
April 1994

Covalent attachment of lipids is a near-universal mechanism through which eukaryotic cells direct and, in some cases, control membrane localization of G proteins. Studies conducted over the past year have substantially advanced our understanding of both the molecular mechanisms and the functional consequences of these modifications. Of particular note are the processes of palmitoylation of the alpha-subunits of heterotrimeric G proteins, and prenylation of members of the Ras superfamily of monomeric G proteins, where recent findings point to unexpected roles for lipid modifications in signaling through these proteins.

Duke Scholars

Published In

Curr Opin Cell Biol

DOI

ISSN

0955-0674

Publication Date

April 1994

Volume

6

Issue

2

Start / End Page

219 / 225

Location

England

Related Subject Headings

  • Protein Processing, Post-Translational
  • Protein Prenylation
  • Palmitic Acids
  • Palmitic Acid
  • Myristic Acids
  • Myristic Acid
  • Molecular Sequence Data
  • Humans
  • GTP-Binding Proteins
  • Fatty Acids
 

Citation

APA
Chicago
ICMJE
MLA
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Casey, P. J. (1994). Lipid modifications of G proteins. Curr Opin Cell Biol, 6(2), 219–225. https://doi.org/10.1016/0955-0674(94)90139-2
Casey, P. J. “Lipid modifications of G proteins.Curr Opin Cell Biol 6, no. 2 (April 1994): 219–25. https://doi.org/10.1016/0955-0674(94)90139-2.
Casey PJ. Lipid modifications of G proteins. Curr Opin Cell Biol. 1994 Apr;6(2):219–25.
Casey, P. J. “Lipid modifications of G proteins.Curr Opin Cell Biol, vol. 6, no. 2, Apr. 1994, pp. 219–25. Pubmed, doi:10.1016/0955-0674(94)90139-2.
Casey PJ. Lipid modifications of G proteins. Curr Opin Cell Biol. 1994 Apr;6(2):219–225.
Journal cover image

Published In

Curr Opin Cell Biol

DOI

ISSN

0955-0674

Publication Date

April 1994

Volume

6

Issue

2

Start / End Page

219 / 225

Location

England

Related Subject Headings

  • Protein Processing, Post-Translational
  • Protein Prenylation
  • Palmitic Acids
  • Palmitic Acid
  • Myristic Acids
  • Myristic Acid
  • Molecular Sequence Data
  • Humans
  • GTP-Binding Proteins
  • Fatty Acids