Key result
Class 1 myosins are monomeric, actin-based motors that remodel the actin network architecture, a higher-order dynamic scaffold that leverages molecular myosin-I functions.
Why the study?
How conformational changes of monomeric myosin-I motors lead to diverse cellular and multicellular phenotypes remains challenging to identify.
Key points are not available for this paper at this time.
Design
Review
May inform cytoskeletal studies in cardiomyocytes; leaves open clinical translation of myosin-I targeting.
The actin cytoskeleton plays crucial roles in cell morphogenesis and functions. The main partners of cortical actin are molecular motors of the myosin superfamily. Although our understanding of myosin functions is heavily based on myosin-II and its ability to dimerize, the largest and most ancient class is represented by myosin-I. Class 1 myosins are monomeric, actin-based motors that regulate a wide spectrum of functions, and whose dysregulation mediates multiple human diseases. We highlight the current challenges in identifying the "pantograph" for myosin-I motors: we need to reveal how conformational changes of myosin-I motors lead to diverse cellular as well as multicellular phenotypes. We review several mechanisms for scaling, and focus on the (re-) emerging function of class 1 myosins to remodel the actin network architecture, a higher-order dynamic scaffold that has potential to leverage molecular myosin-I functions. Undoubtfully, understanding the molecular functions of myosin-I motors will reveal unexpected stories about its big partner, the dynamic actin cytoskeleton.
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Pernier et al. (2022) reported a review. Class 1 myosins are monomeric, actin-based motors that remodel the actin network architecture, a higher-order dynamic scaffold that leverages molecular myosin-I functions.
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