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J Biol Chem, Vol. 273, Issue 32, 20425-20430, August 7, 1998
From the Department of Biological Sciences, University of Notre
Dame, Notre Dame, Indiana 46556
Rab6 is a GTP binding protein that regulates
vesicular trafficking within the Golgi and post-Golgi compartments. We
overexpressed wild-type, a GTPase defective (Q71L), and a guanine
nucleotide binding defective (N125I) Rab6 protein in
Drosophila photoreceptors to assess the in vivo
role of Rab6 in the trafficking of rhodopsin and other proteins.
Expression of Drab6Q71L greatly reduced the
steady state levels of two rhodopsins, Rh1 and Rh3, whereas
Drab6wt and Drab6N125I
showed weaker effects. Analysis of a strain carrying Rh1 rhodopsin under a heat shock promoter showed that
Drab6Q71L, but not
Drab6wt or Drab6N125I,
prevents the maturation of rhodopsin beyond an immature 40 kDa form.
Drab6Q71L is a GTPase defective mutant,
indicating that anterograde transport of rhodopsin requires Rab6 GTPase
function. The three Drab6 strains had no effect on the
expression of several other photoreceptor proteins. The
Drab6Q71L photoreceptors show marked
histological defects at young ages and degenerate over a two week time
span. These results establish that rhodopsin is transported via a Rab6
regulated pathway and that defects in trafficking pathways lead to
retinal degeneration.
Rab6 Regulation of Rhodopsin Transport in
Drosophila
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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