Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase

Beranger, F., Cadwallader, K., Porfiri, E., Powers, S., Evans, T., de Gunzburg, J., Hancock, J. F. (May 1994) Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase. Journal of Biological Chemistry, 269 (18). pp. 13637-43. ISSN 0021-9258

URL: http://www.ncbi.nlm.nih.gov/pubmed/8175798

Abstract

The importance of geranylgeranylation to the interaction of Rab proteins with RabGDI was investigated with a set of Rab6 mutants post-translationally modified by all known C-terminal lipid combinations. Rab6 proteins geranylgeranylated on CXC or CC motifs were found to be significantly better substrates for membrane extraction by RabGDI than either Rab6 proteins geranylgeranylated on CAAL motifs or Rab6 proteins that were farnesylated and palmitoylated. The methylation status of the CXC motif did not significantly affect interaction of wild type Rab6 with RabGDI. Rab6 protein sequences required for RabGDI interaction were then identified. Consistent with the significant homology between Rab-GDI and the Rab escort protein, a subunit of Rab geranylgeranyltransferase (RabGGTase), we show that there is an overlap between Rab6 motifs required for RabGDI binding and RabGGTase processing. The effector domain, loop3/beta 3 and the hypervariable region of Rab6 are all required for RabGDI binding, whereas loop3/beta 3 and the hypervariable region but not the effector domain are required for efficient processing of Rab6 by RabGGTase. Interestingly, however, loop3/beta 3 of Rab6 when introduced into H-Ras is sufficient to allow some in vivo processing of a C-terminal CSC motif.

Item Type: Paper
Uncontrolled Keywords: *Alkyl and Aryl Transferases Amino Acid Sequence Cells, Cultured GTP-Binding Proteins/chemistry/*metabolism *Guanine Nucleotide Dissociation Inhibitors Humans Molecular Sequence Data Protein Processing, Post-Translational Transferases/*metabolism
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GTP binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Rab
CSHL Authors:
Communities: CSHL labs > Powers lab
Depositing User: Matt Covey
Date: 6 May 1994
Date Deposited: 25 Feb 2014 21:08
Last Modified: 25 Feb 2014 21:08
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29523

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