کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2030380 1071095 2006 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The Endosome-Associated Protein Hrs Is Hexameric and Controls Cargo Sorting as a “Master Molecule”
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
The Endosome-Associated Protein Hrs Is Hexameric and Controls Cargo Sorting as a “Master Molecule”
چکیده انگلیسی

SummaryThe 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 14, Issue 4, April 2006, Pages 661–671
نویسندگان
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