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Vol. 12, Issue 8, 2341-2351, August 2001
and
*Department of Neuroscience, University of Connecticut Health
Center, Farmington, Connecticut 06032-3705; Rab8 is a GTPase involved in membrane trafficking. In photoreceptor
cells, rab8 is proposed to participate in the late stages of delivery
of rhodopsin-containing post-Golgi membranes to the plasma membrane
near the base of the connecting cilium. To test the function of rab8 in
vivo, we generated transgenic Xenopus laevis expressing
wild-type, constitutively active (Q67L), and dominant negative (T22N)
forms of canine rab8 in their rod photoreceptors as green fluorescent
protein (GFP) fusion proteins. Wild-type and constitutively active
GFP-rab8 proteins were primarily associated with Golgi and post-Golgi
membranes, whereas the dominant negative protein was primarily
cytoplasmic. Expression of wild-type GFP-rab8 had minimal effects on
cell survival and intracellular structures. In contrast, GFP-rab8T22N
caused rapid retinal degeneration. In surviving peripheral rods,
tubulo-vesicular structures accumulated at the base of the connecting
cilium. Expression of GFP-rab8Q67L induced a slower retinal
degeneration in some tadpoles. Transgene effects were transmitted to F1
offspring. Expression of the GFP-rab8 fusion proteins appears to
decrease the levels of endogenous rab8 protein. Our results demonstrate
a role for rab8 in docking of post-Golgi membranes in rods, and
constitute the first report of a transgenic X. laevis
model of retinal degenerative disease.
Institute of
Biotechnology, University of Helsinki, Finland; and
§Department of Ophthalmology and Visual Sciences and
Cell and Developmental Biology, University of Michigan,
Ann Arbor, Michigan 48105
Corresponding author. E-mail address:
omoritz{at}neuron.uchc.edu.
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