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Rabring7, a Novel Rab7 Target Protein with a RING Finger Motif

Mizuno, Kouichi, Kitamura, Akiko, Sasaki, Takuya·2003·Molecular Biology of the Cell
DOI 10.1091/mbc.e02-08-0495
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Abstract

Rab7, a member of the Rab family small G proteins, has been shown to regulate intracellular vesicle traffic to late endosome/lysosome and lysosome biogenesis, but the exact roles of Rab7 are still undetermined. Accumulating evidence suggests that each Rab protein has multiple target proteins that function in the exocytic/endocytic pathway. We have isolated a new Rab7 target protein, Rabring7 (Rab7-interacting RING finger protein), using a CytoTrap system. It contains an H2 type RING finger motif at the C termini. Rabring7 shows no homology with RILP, which has been reported as another Rab7 target protein. GST pull-down and coimmunoprecipitation assays demonstrate that Rabring7 specifically binds the GTP-bound form of Rab7 at the N-terminal portion. Rabring7 is found mainly in the cytosol and is recruited efficiently to late endosomes/lysosomes by the GTP-bound form of Rab7 in BHK cells. Overexpression of Rabring7 not only affects epidermal growth factor degradation but also causes the perinuclear aggregation of lysosomes, in which the accumulation of the acidotropic probe LysoTracker is remarkably enhanced. These results suggest that Rabring7 plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis.

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Metadata

Authors
Mizuno, K., Kitamura, A., & Sasaki, T.
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2003-09
Volume
14
Issue
9
Pages
3741-3752
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e02-08-0495
Cited by
82
References
1
Language
en

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