The effector domain of Rab6, plus a highly hydrophobic C terminus, is required for Golgi apparatus localization

Beranger, F., Paterson, H., Powers, S., de Gunzburg, J., Hancock, J. F. (January 1994) The effector domain of Rab6, plus a highly hydrophobic C terminus, is required for Golgi apparatus localization. Mol Cell Biol, 14 (1). pp. 744-58. ISSN 0270-7306 (Print)0270-7306

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URL: http://www.ncbi.nlm.nih.gov/pubmed/8264642
DOI: 10.1128/MCB.14.1.744

Abstract

C-terminal lipid modifications are essential for the interaction of Ras-related proteins with membranes. While all Ras proteins are farnesylated and some palmitoylated, the majority of other Ras-related proteins are geranylgeranylated. One such protein, Rab6, is associated with the Golgi apparatus and has a C-terminal CXC motif that is geranylgeranylated on both cysteines. We show here that farnesylation alone cannot substitute for geranylgeranylation in targeting Rab6 to the Golgi apparatus and that whereas Ras proteins that are farnesylated and palmitoylated are targeted to the plasma membrane, mutant Rab proteins that are both farnesylated and palmitoylated associate with the Golgi apparatus. Using chimeric Ras-Rab proteins, we find that there are sequences in the N-terminal 71 amino acids of Rab6 which are required for Golgi complex localization and show that these sequences comprise or include the effector domain. The C-terminal hypervariable domain is not essential for the Golgi complex targeting of Rab6 but is required to prevent prenylated and palmitoylated Rab6 from localizing to the plasma membrane. Functional analysis of these mutant Rab6 proteins in Saccharomyces cerevisiae shows that wild-type Rab6 and C-terminal mutant Rab6 proteins which localize to the Golgi apparatus in mammalian cells can complement the temperature-sensitive phenotype of ypt6 null mutants. Interestingly, therefore, the C-terminal hypervariable domain of Rab6 is not required for this protein to function in S. cerevisiae.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Binding Sites/genetics Cell Line Dogs Fluorescent Antibody Technique Genetic Complementation Test Golgi Apparatus/*metabolism Mice Molecular Sequence Data Mutagenesis, Site-Directed Protein Processing, Post-Translational Proto-Oncogene Proteins p21(ras)/chemistry/genetics/*metabolism Recombinant Fusion Proteins/chemistry/genetics/metabolism Saccharomyces cerevisiae/genetics/metabolism Transformation, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein
organs, tissues, organelles, cell types and functions > organelles, types and functions > golgi
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Rab
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Ras
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Powers lab
Depositing User: Matt Covey
Date: January 1994
Date Deposited: 25 Feb 2014 21:13
Last Modified: 25 Feb 2014 21:13
PMCID: PMC358423
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29524

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