Journal
NATURE GENETICS
Volume 28, Issue 1, Pages 64-68Publisher
NATURE AMERICA INC
DOI: 10.1038/ng0501-64
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Loss of the human 1mucolipin-l gene underlies mucolipidosis type IV (MLIV), a lysosomal storage disease that results in severe developmental neuropathology(1-3). Unlike other lysosomal storage diseases, MLIV is not associated with a lack of lysosomal hydrolases(4); instead, MLIV cells display abnormal endocytosis of lipids and accumulate large vesicles, indicating that a defect in endocytosis may underlie the disease(4-6). Here we report the identification of a loss-of-function mutation in the Caenorhabditis elegans mucolipin-1 homolog, cup-5, and show that this mutation results in an enhanced rate of uptake of fluid-phase markers, decreased degradation of endocytosed protein and accumulation of large vacuoles. Overexpression of cup-5(+) causes the opposite phenotype, indicating that cup-5 activity controls aspects of endocytosis. Studies in model organisms such as C. elegans have helped illuminate fundamental mechanisms involved in normal cellular function and human disease; thus the C. elegans cup-5 mutant may be a useful model for studying conserved aspects of mucolipin-1 structure and function and for assessing the effects of potential therapeutic compounds.
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