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. 1991 Mar;10(3):641–646. doi: 10.1002/j.1460-2075.1991.tb07992.x

Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B).

J F Hancock 1, K Cadwallader 1, C J Marshall 1
PMCID: PMC452695  PMID: 2001678

Abstract

Plasma membrane targeting of p21K-ras(B) requires a CAAX motif and a polybasic domain. The CAAX box directs a triplet of post-translational modifications: farnesylation, proteolysis of the AAX amino acids and methylesterification. These modifications are closely coupled in vivo. However, in vitro translation of mRNA in rabbit reticulocyte lysates produces p21K-ras(B) proteins which are arrested in processing after farnesylation. Intracellular membranes are then required both for proteolytic removal of the AAX amino acids and methylesterification of farnesylated p21K-ras(B). Binding of p21K-ras(B) to plasma membranes in vitro can then be shown to depend critically on AAX proteolysis and methylesterification since p21K-ras(B) which is farnesylated, but not methylated, binds inefficiently to membranes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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