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Vol. 11, Issue 2, 747-763, February 2000
and
*Department of Cell Biology, National Institute for Basic Biology,
Okazaki 444-8585, Japan; The mouse SKD1 is an AAA-type ATPase homologous to the yeast Vps4p
implicated in transport from endosomes to the vacuole. To elucidate a
possible role of SKD1 in mammalian endocytosis, we generated a mutant
SKD1, harboring a mutation (E235Q) that is equivalent to the
dominant negative mutation (E233Q) in Vps4p. Overexpression of the
mutant SKD1 in cultured mammalian cells caused defect in uptake of
transferrin and low-density lipoprotein. This was due to loss of their
receptors from the cell surface. The decrease of the surface
transferrin receptor (TfR) was correlated with expression levels of the
mutant protein. The mutant protein displayed a perinuclear punctate
distribution in contrast to a diffuse pattern of the wild-type SKD1.
TfR, the lysosomal protein lamp-1, endocytosed dextran, and epidermal
growth factor but not markers for the secretory pathway were
accumulated in the mutant SKD1-localized compartments. Degradation of
epidermal growth factor was inhibited. Electron microscopy revealed
that the compartments were exaggerated multivesicular vacuoles with
numerous tubulo-vesicular extensions containing TfR and endocytosed
horseradish peroxidase. The early endosome antigen EEA1 was also
redistributed to these aberrant membranes. Taken together, our findings
suggest that SKD1 regulates morphology of endosomes and membrane
traffic through them.
Department of Biosciences,
Teikyo University of Science and Technology, Yamanashi 409-0193, Japan;
§Department of Physiology, Kansai Medical University,
Moriguchi 570-0074, Japan; PRESTO, Japan Science and
Technology Corporation, Okazaki 444-8585, Japan; and
¶Department of Molecular Physiology, National Institute
for Physiological Sciences, Okazaki 444-8585, Japan
Corresponding author. E-mail address:
yosimori{at}nibb.ac.jp.
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