The endosome-associated protein Hrs is hexameric and controls cargo sorting as a "master molecule".
The structure of the endosomal-associated protein, Hrs, has been determined with cryo-electron microscopy. Hrs interacts with a number of proteins, including SNAP-25 and STAM1, forming a complex that binds ubiquitin moieties. Analytical ultracentrifugation studies revealed that Hrs exists as a hexamer. The symmetry and the structure of the hexameric form ... of Hrs were determined with the single-particle reconstruction method. Hrs comprises three antiparallel dimers with a central core and distinct caps on either end. Crystal structures of VHS and FYVE domains fit into the Hrs end caps in the EM density map. Thus, the location of domains that interact with the endosomal membrane, the VHS, FYVE, and C-terminal domains, facilitates the anchorage of Hrs to the membrane, initiating the functional processes of Hrs on the endosome. Based on our model, the Hrs hexamer interacts with the membrane and acts as a "master molecule" that presents multiple sites for protein binding.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Chromatography, Gel, Cryoelectron Microscopy, Crystallography, X-Ray, Dimerization, Dose-Response Relationship, Drug, Endosomal Sorting Complexes Required for Transport, Endosomes, HeLa Cells, Humans, Image Processing, Computer-Assisted, Insects, Mice, Microscopy, Electron, Models, Molecular, Molecular Sequence Data, Phosphoproteins, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Protein Transport, Proteins, Synaptosomal-Associated Protein 25, Ultracentrifugation
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Cell Line, Cell Membrane, Chromatography, Gel, Cryoelectron Microscopy, Crystallography, X-Ray, Dimerization, Dose-Response Relationship, Drug, Endosomal Sorting Complexes Required for Transport, Endosomes, HeLa Cells, Humans, Image Processing, Computer-Assisted, Insects, Mice, Microscopy, Electron, Models, Molecular, Molecular Sequence Data, Phosphoproteins, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Protein Transport, Proteins, Synaptosomal-Associated Protein 25, Ultracentrifugation
Structure
Date: Apr. 01, 2006
PubMed ID: 16615908
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