The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain.
The mammalian retromer complex consists of SNX1, SNX2, Vps26, Vps29 and Vps35, and retrieves lysosomal enzyme receptors from endosomes to the trans-Golgi network. The structure of human Vps26A at 2.1-A resolution reveals two curved beta-sandwich domains connected by a polar core and a flexible linker. Vps26 has an unpredicted structural relationship to arrestins. The Vps35- binding site on Vps26 maps to a mobile loop spanning residues 235-246, near the tip of the C-terminal domain. The loop is phylogenetically conserved and provides a mechanism for Vps26 integration into the complex that leaves the rest of the structure free for engagements with membranes and for conformational changes. Hydrophobic residues and a glycine in this loop are required for integration into the retromer complex and endosomal localization of human Vps26, and for the function of yeast Vps26 in carboxypeptidase Y sorting.[1]References
- The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain. Shi, H., Rojas, R., Bonifacino, J.S., Hurley, J.H. Nat. Struct. Mol. Biol. (2006) [Pubmed]
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