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Vol. 12, Issue 7, 2011-2021, July 2001
Department of Biochemistry and Molecular Biophysics, Columbia
University, College of Physicians and Surgeons, New York, New York
10032
By genetic analysis of Caenorhabditis elegans
mutants defective in yolk uptake, we have identified new molecules
functioning in the endocytosis pathway. Here we describe a novel
J-domain-containing protein, RME-8, identified by such genetic
analysis. RME-8 is required for receptor-mediated endocytosis and
fluid-phase endocytosis in various cell types and is essential for
C. elegans development and viability. In the
macrophage-like coelomocytes, RME-8 localizes to the limiting membrane
of large endosomes. Endocytosis markers taken up by the coelomocytes
rapidly accumulate in these large RME-8-positive endosomes,
concentrate in internal subendosomal structures, and later appear in
RME-8-negative lysosomes. rme-8 mutant coelomocytes
fail to accumulate visible quantities of endocytosis markers. These
observations show that RME-8 functions in endosomal trafficking before
the lysosome. RME-8 homologues are found in multicellular organisms
from plants to humans but not in the yeast Saccharomyces
cerevisiae. These sequence homologies suggest that RME-8
fulfills a conserved function in multicellular organisms.
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