Key result
External loads asymmetrically affect ADP affinity in myosins V and VI, with forward loads modestly accelerating and backward loads inhibiting ADP dissociation, generating an intramolecular load of ~2 pN.
Population
Individual actomyosin V or VI bonds
Comparison
External loads applied to individual actomyosin… vs Forward vs backward loads
Design
Preclinical
Authors
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Distinct load sensitivities enable specialized myosin roles; leaves open translation to cardiac mechanobiology.
The distinct load dependence of ADP binding allows myosin V and VI to perform different cellular functions.
Oguchi et al. (2008) studied this question. External loads applied to individual actomyosin V or VI bonds was evaluated on ADP affinity and dissociation kinetics. External loads asymmetrically affect ADP affinity in myosins V and VI, with forward loads modestly accelerating and backward loads inhibiting ADP dissociation, generating an intramolecular load of ~2 pN.
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