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Papers In Press, published online ahead of print July 14, 2003
Laboratory of Molecular and Cellular Regulation, Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan 464-8601
Corresponding Author: mmaki{at}agr.nagoya-u.ac.jp
Alix is a 95-kDa protein that interacts with an EF-hand type Ca2+-binding protein, ALG-2, through its C-terminal proline-rich region. The N-terminal two thirds of Alix is highly conserved among its homologues in various organisms from yeast to human, but the function of this region has not yet been elucidated. In this study, we searched for proteins that interact with human Alix
J. Biol. Chem, 10.1074/jbc.M301604200
Submitted on February 14, 2003
Revised on July 14, 2003
Accepted on July 14, 2003
The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
C (a truncated form not containing the C-terminal proline-rich region) by using a yeast two-hybrid screen, and we identified two similar human proteins, CHMP4a and CHMP4b, as novel binding partners of Alix. The interaction of Alix with CHMP4b was further confirmed by a glutathione-S-transferase pull-down assay and by co-immunoprecipitation experiments. Fluorescence microscopic analysis using CHMP4b that was either epitope-tagged or fused with green fluorescent protein (GFP) revealed that CHMP4b transiently expressed in HeLa cells mainly exhibited a punctate distribution in the perinuclear area and co-localized with co-expressed Alix. The distribution of CHMP4b partly overlapped the distributions of early and late endosomal marker proteins, EEA1 and Lamp-1, respectively. Transient overexpression of CHMP4b induced the accumulation of ubiquitinated proteins as punctate patterns that were partly overlapped with the distribution of CHMP4b, and inhibited the disappearance of endocytosed epidermal growth factor. In contrast, stably expressed CHMP4b in HEK293 cells was observed diffusely in the cytoplasm. Transient overexpression of AlixC in stably CHMP4b-expressing cells, however, induced formation of vesicle-like structures in which CHMP4b and AlixC were co-localized. SKD1E235Q, a dominant negative form of the AAA type ATPase SKD1 that plays critical roles in the endocytic pathway, was co-immunoprecipitated with CHMP4b. Furthermore, CHMP4b co-localized with SKD1E235Q as punctate patterns in the perinuclear area, and Alix was induced to exhibit dot-like distributions overlapped with SKD1E235Qin HeLa cells. These results suggest that CHMP4b and Alix participate in formation of multivesicular bodies by co-operating with SKD1.
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