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Vol. 10, Issue 4, 847-859, April 1999
Center for Basic Neuroscience, Department of Cell Biology and
Neuroscience, University of Texas Southwestern Medical Center, Dallas,
Texas 75235-9111
Mutations in the hook gene alter intracellular
trafficking of internalized ligands in Drosophila. To
dissect this defect in more detail, we developed a new approach to
visualize the pathway taken by the Bride of Sevenless (Boss) ligand
after its internalization into R7 cells. A chimeric protein consisting
of HRP fused to Boss (HRP-Boss) was expressed in R8 cells. This
chimera was fully functional: it rescued the boss mutant
phenotype, and its trafficking was indistinguishable from that of the
wild-type Boss protein. The HRP activity of the chimera was used to
follow HRP-Boss trafficking on the ultrastructural level through early
and late endosomes in R7 cells. In both wild-type and
hook mutant eye disks, HRP-Boss was internalized
into R7 cells. In wild-type tissue, Boss accumulated in mature
multivesicular bodies (MVBs) within R7 cells; such accumulation was not
observed in hook eye disks, however. Quantitative
electron microscopy revealed a loss of mature MVBs in
hook mutant tissue compared with wild type, whereas more
than twice as many multilammelar late endosomes were detected. Our
genetic analysis indicates that Hook is required late in endocytic
trafficking to negatively regulate delivery from mature MVBs to
multilammelar late endosomes and lysosomes.
Corresponding author. E-mail address:
KRAMER{at}UTSW.SWMED.EDU.
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