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Vol. 11, Issue 12, 4105-4116, December 2000
Diabetes Branch, National Institutes of Diabetes and Digestive and
Kidney Diseases, National Institutes of Health, Bethesda, Maryland
20892-1770
Sorting nexin (SNX) 1 and SNX2 are mammalian orthologs of Vps5p, a
yeast protein that is a subunit of a large multimeric complex, termed
the retromer complex, involved in retrograde transport of proteins from
endosomes to the trans-Golgi network. We report the
cloning and characterization of human orthologs of three additional components of the complex: Vps26p, Vps29p, and Vps35p. The close structural similarity between the yeast and human proteins suggests a
similarity in function. We used both yeast two-hybrid assays and
expression in mammalian cells to define the binding interactions among
these proteins. The data suggest a model in which hVps35 serves as the
core of a multimeric complex by binding directly to hVps26, hVps29, and
SNX1. Deletional analyses of hVps35 demonstrate that amino acid
residues 1-53 and 307-796 of hVps35 bind to the coiled
coil-containing domain of SNX1. In contrast, hVps26 binds to amino acid
residues 1-172 of hVps35, whereas hVps29 binds to amino acid residues
307-796 of hVps35. Furthermore, hVps35, hVps29, and hVps26 have been
found in membrane-associated and cytosolic compartments. Gel filtration
chromatography of COS7 cell cytosol showed that both recombinant and
endogenous hVps35, hVps29, and hVps26 coelute as a large complex
(~220-440 kDa). In the absence of hVps35, neither hVps26 nor hVps29
is found in the large complex. These data provide the first insights
into the binding interactions among subunits of a putative mammalian
retromer complex.
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