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Related Concept Videos

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...
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,...
The Role of Actin and Myosin in Non-muscle Cells01:10

The Role of Actin and Myosin in Non-muscle Cells

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...
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...
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...

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

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Published on: February 4, 2021

Cargo binding activates myosin VIIA motor function in cells.

Tsuyoshi Sakai1, Nobuhisa Umeki, Reiko Ikebe

  • 1Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, MA 01655, USA.

Proceedings of the National Academy of Sciences of the United States of America
|April 13, 2011
PubMed
Summary
This summary is machine-generated.

Myosin VIIA dimer formation is crucial for cargo transport, as shown by its movement to filopodia tips. Cargo molecules like MyRip/Rab27a also activate myosin VIIA

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Area of Science:

  • Cell biology
  • Molecular motor function
  • Genetics of hearing and vision loss

Background:

  • Myosin VIIA is implicated in human auditory function and Usher syndrome type 1B, causing hearing and visual loss.
  • Myosin VIIA is known to exist as a monomer in vitro, unlike processive myosin Va.
  • The mechanism activating myosin VIIA as a cargo-transporting motor is currently unknown.

Purpose of the Study:

  • To investigate the molecular mechanism of myosin VIIA activation for cargo transport.
  • To determine the role of dimer formation in myosin VIIA's motor activity.
  • To understand how cargo molecules influence myosin VIIA's function.

Main Methods:

  • Utilizing dimer-inducing reagents to induce myosin VIIA dimerization.
  • Observing myosin VIIA localization and cargo (MyRip) translocation in filopodia.
  • Investigating the effect of cargo complex (MyRip/Rab27a) on myosin VIIA translocation.
  • Analyzing coexpression of MyRip to study its effect on myosin VIIA-vesicle association and dimer formation.

Main Results:

  • Forced dimerization of myosin VIIA caused its translocation to filopodial tips, along with its cargo molecule MyRip.
  • Myosin VIIA lacking forced dimerization did not translocate to filopodial tips without cargo.
  • Myosin VIIA monomers associated with the MyRip/Rab27a cargo complex translocated to filopodial tips.
  • Coexpression of MyRip promoted myosin VIIA association with vesicles and induced dimer formation, suggesting membrane association facilitates dimerization and transport.

Conclusions:

  • Dimer formation is essential for activating myosin VIIA's cargo-transporting activity.
  • Cargo molecules, particularly the MyRip/Rab27a complex, act as activators by facilitating myosin VIIA's association with membranes and promoting dimer formation.
  • MyRip functions as a key activator for myosin VIIA transporter function, likely through enabling dimerization upon cargo binding.