Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 3, Pages 295-U78Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1985
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Funding
- Human Frontier Science Program Organization
- Swiss National Science Foundation
- US National Institutes of Health (NIH) [GM-073165]
- NIH (New England Regional Center of Excellence in Biodefense and Emerging Infectious Disease, Core Imaging Facility) [GM-075252, U54 AI057159]
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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.
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