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. 2007 Apr 23;177(2):205–210. doi: 10.1083/jcb.200607084

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Copyright © 2007, The Rockefeller University Press

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Figure 4. — Mechanism of UNC-45 chaperone–mediated proteasomal degradation of myosin. (A) Myosin assembly as an idealized function of UNC-45 chaperone levels. The two are linked by control of myosin accumulation through its degradation. ts, temperature sensitive. (B) Proposed mechanism of UNC-45 chaperone–mediated myosin assembly, disassembly, and consequent degradation. All reactions represented by opposing arrows are reversible; myosin degradation represented by a single arrow is irreversible. By mass action, chaperone deficiency leads to a buildup of free, nonnative myosin, a substrate for the proteasome. Similarly, excess chaperone leads to a buildup of its complexes with myosin molecules and filaments. These complexes lead to increased levels of free, nonnative myosin and its proteasomal degradation.