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Post-translational modifications of p21rho proteins.

Adamson, P, Marshall, C.J., Hall, A, Tilbrook, P.A.·1992·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)88661-1
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Abstract

Post-translational modifications of the ras proteins, which are required for plasma membrane localization and biological function of the proteins, have been shown to include prenylation and carboxymethylation at the carboxyl terminal cysteine residue of the cysteine-aliphatic amino acid-aliphatic amino acid-any amino acid (CAAX) box. In addition, p21Ha-ras and p21N-ras, but not p21K-ras (B), are palmitoylated. The three mammalian rho proteins (A, B, and C) are also members of the ras superfamily but have distinct biological activities and different intracellular distributions from p21ras. Analysis showed all three rho proteins are modified by a COOH-terminal carboxymethylation similar to p21ras, whereas p21rhoC labeled with [3H]mevalonic acid in vivo revealed the presence of a C20 prenoid, similar to that already described for p21rhoA. However, in vivo and in vitro studies of p21rhoB showed this protein to be modified by both C15 and C20 prenoids. Mutation of C193 in the CAAX box abolished prenylation, whereas mutation of the adjacent C192 resulted in a significant reduction in the amount of the C20, but not C15 prenoid, recovered from p21rhoB. In vivo labeling studies with [3H]palmitic acid and mutational analysis showed that both cysteine residues at 189 and 192 upstream of the CAAX box in p21rhoB are sites for palmitoylation. We conclude that there are different populations of post-translationally modified p21rhoB in the cell and that the sequence specificity for geranylge…

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Metadata

Authors
Adamson, P., Marshall, C. J., Hall, A., & Tilbrook, P. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1992-10
Volume
267
Issue
28
Pages
20033-20038
ISSN
0021-9258
DOI
10.1016/s0021-9258(19)88661-1
Cited by
335
References
0
Language
en
Licence

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