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Isoprenoid modification of rab proteins terminating in cc or cxc motifs

Academic Article
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Overview

authors

  • Khosravifar, R.
  • Lutz, R. J.
  • Cox, A. D.
  • Conroy, L.
  • Bourne, J. R.
  • Sinensky, M.
  • Balch, William E.
  • Buss, J. E.
  • Der, C. J.

publication date

  • July 1991

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Mevalonate starvation of hamster fibroblasts resulted in a shift of rab1b from the membrane to the cytosolic fraction, suggesting that rab1b depends upon an isoprenoid modification for its membrane localization. rab1b and rab3a proteins expressed in insect cells incorporated a product of [3H]mevalonate, and gas chromatography analysis of material released by Raney nickel cleavage demonstrated that rab1b and rab3a are modified by geranylgeranyl groups. Additionally, in vitro prenylation analysis demonstrated farnesyl modification of H-ras but geranylgeranyl modification of five rab proteins (1a, 1b, 2, 3a, and 6). Together, these results suggest that the carboxyl-terminal CC/CXC motifs (X = any amino acid) specifically signal for addition of geranylgeranyl, but not farnesyl, groups. A rab1b mutant protein lacking the two carboxyl-terminal cysteine residues was not prenylated in vitro. However, since a mutant H-ras protein that terminates with tandem cysteine residues was also not modified, the CC motif may be essential, but not sufficient, to signal prenylation of rab1b. Finally, rab1b and rab3a proteins were not efficient substrates for either farnesyl- or geranylgeranyltransferase activities that modify CAAX-containing proteins (A = any aliphatic amino acid). Therefore, rab proteins may be modified by a prenyltransferase(s) distinct from the prenyltransferases that modify carboxyl-terminal CAAX proteins.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Codon
  • Cricetinae
  • Escherichia coli
  • GTP-Binding Proteins
  • Insecta
  • Mevalonic Acid
  • Nerve Tissue Proteins
  • Polyisoprenyl Phosphates
  • Protein Processing, Post-Translational
  • Recombinant Proteins
  • rab1 GTP-Binding Proteins
  • rab3 GTP-Binding Proteins
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Research

keywords

  • MEMBRANE ASSOCIATION
  • RAS-RELATED PROTEINS
  • VESICULAR TRANSPORT
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Identity

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.88.14.6264

PubMed ID

  • 1648736
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Additional Document Info

start page

  • 6264

end page

  • 6268

volume

  • 88

issue

  • 14

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