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Related Concept Videos

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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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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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.
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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
08:04

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Published on: January 26, 2019

Motor proteins: kinesin can replace Myosin.

Kathleen Scheffler1, Phong T Tran

  • 1Institut Curie, CNRS-UMR144, Paris 75005, France.

Current Biology : CB
|January 28, 2012
PubMed
Summary
This summary is machine-generated.

Researchers engineered a kinesin motor protein to perform the functions of myosin V, demonstrating its ability to transport specific cellular cargos along actin tracks and enabling crucial cellular processes.

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Area of Science:

  • Cell Biology
  • Molecular Motors
  • Cytoskeletal Dynamics

Background:

  • Directional transport of cellular cargos relies on specific molecular motors (like myosin V, kinesin, dynein) and their corresponding cytoskeletal tracks (actin filaments or microtubules).
  • Myosin V utilizes actin tracks, while kinesin and dynein utilize microtubules for cargo transport.

Purpose of the Study:

  • To investigate if an engineered kinesin motor could functionally replace myosin V.
  • To determine if this engineered motor could mediate cargo-specific transport and cellular functions typically performed by myosin V.

Main Methods:

  • Protein engineering to create a novel kinesin motor.
  • In vitro and in vivo assays to assess cargo binding and transport capabilities.
  • Functional assays to evaluate cellular processes dependent on myosin V.

Main Results:

  • The engineered kinesin successfully bound to and transported specific cargos normally handled by myosin V.
  • The engineered motor demonstrated the ability to mediate essential cellular functions previously dependent on myosin V.
  • This engineered motor protein showed adaptability in utilizing actin tracks, a departure from native kinesin.

Conclusions:

  • Engineered kinesin motors can be designed to substitute for other motor proteins like myosin V.
  • This demonstrates the potential for synthetic biology approaches to engineer molecular machinery for specific cellular tasks.
  • The study highlights the plasticity of cytoskeletal transport systems and the potential for novel motor functions.