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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.
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

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 cargos...
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

Role of Myosin in Cell Migration

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.
Myosin II  is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction. It is...
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...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

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Related Experiment Video

Updated: Jun 21, 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

Myosin VI undergoes cargo-mediated dimerization.

Cong Yu1, Wei Feng, Zhiyi Wei

  • 1Department of Biochemistry, Molecular Neuroscience Center, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong.

Cell
|August 12, 2009
PubMed
Summary
This summary is machine-generated.

Myosin VI motor protein converts from a monomer to a dimer upon binding cargo, like Dab2. This cargo-binding-induced dimerization regulates its unique minus-end directed movement along actin filaments.

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Last Updated: Jun 21, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
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Published on: February 14, 2016

Area of Science:

  • Molecular Biology
  • Cellular Biophysics
  • Structural Biology

Background:

  • Myosin VI is a unique molecular motor moving towards the minus ends of actin filaments, essential for various cellular functions.
  • Myosin VI's processive movement relies on dimerization, yet the mechanism of monomer-dimer conversion remains unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism regulating monomer-dimer conversion in Myosin VI.
  • To investigate the role of cargo binding in Myosin VI's functional regulation.

Main Methods:

  • Determined the high-resolution NMR structure of the cargo-free Myosin VI cargo-binding domain (CBD).
  • Characterized the interaction between Myosin VI CBD and a Dab2 protein fragment.
  • Resolved the X-ray structure of the Myosin VI CBD-Dab2 complex.

Main Results:

  • The cargo-free Myosin VI CBD exists as a stable monomer in solution.
  • Myosin VI CBD binds with high affinity to a fragment of the adaptor protein Dab2.
  • X-ray crystallography revealed cargo binding induces dimerization of the Myosin VI CBD.

Conclusions:

  • Cargo-binding-induced dimerization is a key mechanism regulating Myosin VI activity and processivity.
  • This dimerization paradigm may extend to other myosins, such as Myosin VII and Myosin X.