April 7, 2000Science
The Way Things Move: Looking Under the Hood of Molecular Motor Proteins
Key result
Kinesin and myosin share a common core structure and convert energy from ATP into protein motion using a similar conformational change strategy despite diverse motile properties.
Population
Molecular motor proteins (microtubule-based kinesin motors and actin-based myosin motors)
Design
Review
Authors
Discussion
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Member takes
Implication
Informs mechanistic studies of cardiac contractility; leaves open therapeutic targeting in cardiomyopathy.
Key Points
- To review the structural and mechanical principles governing motility in kinesin and myosin molecular motor proteins.
- Comparative structural and mechanistic review of microtubule-associated kinesins and actin-associated myosins.
- Kinesin and myosin share a conserved structural catalytic core despite divergent evolutionary lineages and track specificities.
- Both motor families utilize a homologous conformational change strategy to couple adenosine triphosphate hydrolysis with mechanical force generation.
- Diverse biological functions across cell division, transport, and muscle contraction arise from distinct mechanical amplifiers coupled to the conserved engine core.
Structured PICO
P
Population
Molecular motor proteins (microtubule-based kinesin motors and actin-based myosin motors)
Kinesin and myosin share a common core structure and mechanism for converting ATP into motion, despite earlier beliefs that they worked by different mechanisms.
Cite This Study
Vale et al. (2000) conducted a review in Molecular motor proteins. Kinesin and myosin share a common core structure and convert energy from ATP into protein motion using a similar conformational change strategy despite diverse motile properties.