Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1) |
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Authors: | Lee Hyung Ho Nemecek Daniel Schindler Christina Smith William J Ghirlando Rodolfo Steven Alasdair C Bonifacino Juan S Hurley James H |
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Institution: | Department of Bio and Nano Chemistry, Kookmin University, Seoul 136-702, Korea. |
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Abstract: | BLOC-1 (biogenesis of lysosome-related organelles complex-1) is critical for melanosome biogenesis and has also been implicated in neurological function and disease. We show that BLOC-1 is an elongated complex that contains one copy each of the eight subunits pallidin, Cappuccino, dysbindin, Snapin, Muted, BLOS1, BLOS2, and BLOS3. The complex appears as a linear chain of eight globular domains, ~300 ? long and ~30 ? in diameter. The individual domains are flexibly connected such that the linear chain undergoes bending by as much as 45°. Two stable subcomplexes were defined, pallidin-Cappuccino-BLOS1 and dysbindin-Snapin-BLOS2. Both subcomplexes are 1:1:1 heterotrimers that form extended structures as indicated by their hydrodynamic properties. The two subcomplexes appear to constitute flexible units within the larger BLOC-1 chain, an arrangement conducive to simultaneous interactions with multiple BLOC-1 partners in the course of tubular endosome biogenesis and sorting. |
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Keywords: | Lysosomes Protein Complexes Protein Structure SNARE Proteins Trafficking |
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