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Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating
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Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating
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Journal Article
Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating
2011
Overview
Hsc70 disassembles the coats of clathrin-coated vesicles, remodels a number of other protein complexes, and facilitates protein folding. The dynamics of clathrin uncoating promoted by Hsc70 have now been monitored with single-particle fluorescence imaging. The results suggest that disassembly is driven by trapping of small conformational fluctuations.
Heat shock cognate protein-70 (Hsc70) supports remodeling of protein complexes, such as disassembly of clathrin coats on endocytic coated vesicles. To understand how a simple ATP-driven molecular clamp catalyzes a large-scale disassembly reaction, we have used single-particle fluorescence imaging to track the dynamics of Hsc70 and its clathrin substrate in real time. Hsc70 accumulates to a critical level, determined by kinetic modeling to be one Hsc70 for every two functional attachment sites; rapid, all-or-none uncoating then ensues. We propose that Hsc70 traps conformational distortions, seen previously by cryo-EM, in the vicinity of each occupied site and that accumulation of local strains destabilizes the clathrin lattice. Capture of conformational fluctuations may be a general mechanism for chaperone-driven disassembly of protein complexes.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Adenosine Triphosphate - metabolism
/ Animals
/ ATP
/ Biomedical and Life Sciences
/ Cattle
/ Clathrin
/ Clathrin-Coated Vesicles - chemistry
/ Clathrin-Coated Vesicles - genetics
/ Clathrin-Coated Vesicles - metabolism
/ HSC70 Heat-Shock Proteins - chemistry
/ HSC70 Heat-Shock Proteins - genetics
/ HSC70 Heat-Shock Proteins - metabolism
/ Kinetics
/ Mutation
/ Rats
