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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well...
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Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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Related Experiment Video

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Author Spotlight: Unraveling the Role of Myosin-7a and Usher Proteins in Hearing and Human Disease
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A binding protein regulates myosin-7a dimerization and actin bundle assembly.

Rong Liu1, Neil Billington1, Yi Yang1,2

  • 1Laboratory of Molecular Physiology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD, 20892, USA.

Nature Communications
|January 26, 2021
PubMed
Summary
This summary is machine-generated.

Researchers discovered M7BP, a protein that activates myosin-7a. This myosin-7a-M7BP complex forms motile structures, enabling cargo transport and remodeling the actin cytoskeleton for cell protrusions.

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Area of Science:

  • Cell Biology
  • Molecular Motors
  • Cytoskeleton Dynamics

Background:

  • Myosin-7a is a monomeric motor protein involved in organizing actin-based cell protrusions like filopodia and stereocilia.
  • It also plays a role in cargo transport within these cellular structures.

Purpose of the Study:

  • To identify binding partners of Drosophila myosin-7a.
  • To elucidate the mechanism by which myosin-7a is assembled into a functional motile complex.
  • To understand the role of this complex in actin cytoskeletal remodeling and cargo translocation.

Main Methods:

  • Protein binding assays to identify M7BP as a myosin-7a binding partner.
  • Biochemical and single-molecule reconstitution experiments to analyze complex formation and motility.
  • In vivo imaging in living cells to observe the function of the myosin-7a-M7BP complex.

Main Results:

  • M7BP binds to the autoinhibitory tail of myosin-7a, activating its ATPase activity.
  • M7BP facilitates the formation of 2:2 translocation dimers of myosin-7a, enabling robust, actin-regulated motility.
  • The complex enhances motor processivity by tethering actin filaments and promotes actin alignment.
  • The myosin-7a-M7BP complex is shown to assemble actin bundles and filopodia-like structures, migrating along them in living cells.

Conclusions:

  • M7BP is a crucial assembly factor for myosin-7a, converting it into a processive motor.
  • The myosin-7a-M7BP complex drives actin cytoskeletal organization and dynamics, particularly in cell protrusions.
  • These findings offer new insights into the functional mechanisms of myosin-7a in cellular processes.