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Related Concept Videos

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

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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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Role of Myosin in Cell Migration01:18

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Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Actin and Myosin in Muscle Contraction01:16

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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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Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
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Related Experiment Video

Updated: Aug 5, 2025

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Endocytic myosin-1 is a force-insensitive, power-generating motor.

Ross Ta Pedersen1,2,3, Aaron Snoberger4,3, Serapion Pyrpassopoulos4

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.

Biorxiv : the Preprint Server for Biology
|March 30, 2023
PubMed
Summary
This summary is machine-generated.

Yeast type I myosin, Myo5, generates power during endocytosis rather than acting as a force-sensitive anchor. Phosphorylation significantly activates this motor, influencing its role in cellular processes.

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Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
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Area of Science:

  • Cell Biology
  • Molecular Motors
  • Biophysics

Background:

  • Myosins are crucial for clathrin-mediated endocytosis, but their exact functions remain unclear due to limited biophysical data.
  • Understanding myosin mechanochemistry is key to elucidating their roles in endocytosis.

Approach:

  • Investigated the in vitro force-dependent kinetics of Saccharomyces cerevisiae endocytic type I myosin, Myo5.
  • Analyzed Myo5's working stroke and actin-detachment kinetics under varying forces.

Key Points:

  • Myo5 exhibits low-duty-ratio motor activity.
  • Phosphorylation activates Myo5 approximately 10-fold.
  • Myo5's kinetics are largely force-insensitive, resembling cardiac myosin more than anchoring myosins.

Conclusions:

  • Myo5 likely generates power to enhance actin assembly forces during endocytosis.
  • This study provides novel insights into the mechanochemical properties of Myo5.
  • The findings suggest a power-generating role for Myo5 in cellular endocytic events.