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Related Concept Videos

Overview of Myosin Structure and Function01:15

Overview of Myosin Structure and Function

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 characterized.
The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

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,...
Role of Myosin in Cell Migration01:18

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Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
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Related Experiment Video

Updated: Jul 14, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
08:57

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays

Published on: February 4, 2021

How myosin VI coordinates its heads during processive movement.

H Lee Sweeney1, Hyokeun Park, Alan B Zong

  • 1Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA, USA.

The EMBO Journal
|May 19, 2007
PubMed
Summary

Myosin VI uses a unique gating mechanism, blocking ATP binding to its lead head after ADP release, to ensure processive movement along actin tracks. This differs from other myosins and resembles kinesin I.

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Last Updated: Jul 14, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
09:38

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

Published on: July 1, 2021

Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • Processive molecular motors require coordinated enzymatic states in their catalytic domains to maintain track attachment.
  • Myosin V utilizes internal strain to regulate its enzymatic cycle, preventing premature detachment.
  • Myosin VI, with reversed lever arm positions, cannot employ the same strain-dependent mechanism as myosin V.

Purpose of the Study:

  • To elucidate the unique gating mechanism of myosin VI that ensures processivity.
  • To identify the structural basis for myosin VI's distinct regulatory strategy.
  • To compare myosin VI's mechanism with other molecular motors.

Main Methods:

  • Structural analysis of myosin VI.
  • Biochemical assays to study nucleotide binding and release.
  • Comparative analysis with other motor proteins.

Main Results:

  • Myosin VI gating is achieved by blocking ATP binding to the lead head after ADP release.
  • A unique insert near the nucleotide-binding pocket in myosin VI is crucial for this mechanism.
  • Reverse strain favors ADP binding to the lead head, facilitating processivity.

Conclusions:

  • Myosin VI employs a novel gating mechanism distinct from other myosin superfamily members.
  • This mechanism allows myosin VI to function as both a processive transporter and an actin-based anchor.
  • Myosin VI's mechanism shares similarities with kinesin I, suggesting convergent evolution in processive motor function.