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A more recent version of this article appeared on August 1, 2002
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Submitted on May 1, 2002
Accepted on June 5, 2002
1 University of Cambridge, Dept. of Clinical Biochemistry and Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Addenbrookes Hospital, Hills Road, Cambridge, CB2 2XY, UK
2 University of Cambridge, Dept. of Clinical Biochemistry and Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Addenbrookes Hospital, Hills Road, Cambridge, CB2 2XY, UK (present address: MRC Laboratory for Molecular Cell Biology and Dept. of Biology, University College London, Gower Street, London, WC1E 6BT)
* Corresponding author. E-mail address: mnjs100{at}cam.ac.uk.
Sorting Nexins (Snxs) are a recently discovered family of conserved hydrophilic cytoplasmic proteins which have been found associated with membranes of the endocytic system and are implicated in the trafficking of many endosomal membrane proteins including the epidermal growth factor receptor (EGFR) and transferrin receptor (TfnR). Snx proteins are partly defined by the presence of a p40 phox homology (PX) domain which has recently been shown to bind phosphatidylinositol 3-phosphate (PtdIns 3-P). Most Snx proteins also contain a predicted coiled-coils domain in the carboxyl-terminal half of the protein and have been shown to form dimers with other members of the Snx family. The yeast Sorting Nexins Vps5p and Vps17p form a dimer and are also components of the retromer complex that mediates endosome to Golgi transport of the carboxypeptidase Y receptor, Vps10p. To functionally define the different domains of the yeast Sorting Nexins, Vps5p and Vps17p, we have generated various truncations to examine the role that the different domains of Vps5p/Vps17p play in their respective functions. Here we show that the C-terminal halves of Vps5p and Vps17p, which contain the coiled-coils domains, are necessary and sufficient for their interaction. We have also mapped the retromer assembly domain to the N-terminal half of Vps5p and found that binding of Vps5p by Vps17p synergises the interaction between Vps5p and other retromer components. Additionally we have examined which domain(s) of Vps5p is necessary for membrane association.
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