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Videos de Conceptos Relacionados

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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Video Experimental Relacionado

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

La miosina VI sufre una dimerización mediada por la carga.

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
Resumen
Este resumen es generado por máquina.

La proteína motora de miosina VI se convierte de un monómero a un dímero al unirse a la carga, como Dab2. Esta dimerización inducida por la unión de la carga regula su movimiento único dirigido hacia el extremo negativo a lo largo de los filamentos de actina.

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Videos de Experimentos Relacionados

Last Updated: Jun 21, 2026

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

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Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
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Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
08:06

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • La Biofísica Celular es una Biofísica Celular.
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • La miosina VI es un motor molecular único que se mueve hacia los extremos negativos de los filamentos de actina, esenciales para varias funciones celulares.
  • El movimiento procesivo de la miosina VI se basa en la dimerización, sin embargo, el mecanismo de conversión monómero-dimero sigue sin estar claro.

Objetivo del estudio:

  • Para dilucidar el mecanismo molecular que regula la conversión monómero-dimero en la miosina VI.
  • Investigar el papel de la unión de la carga en la regulación funcional de la miosina VI.

Principales métodos:

  • Se determinó la estructura de RMN de alta resolución del dominio de unión de carga (CBD) de la miosina VI libre de carga.
  • Caracterizó la interacción entre Myosin VI CBD y un fragmento de proteína Dab2.
  • Se resolvió la estructura de rayos X del complejo Myosin VI CBD-Dab2.

Principales resultados:

  • El Myosin VI CBD sin carga existe como un monómero estable en solución.
  • La miosina VI CBD se une con alta afinidad a un fragmento de la proteína adaptadora Dab2.
  • La cristalografía de rayos X reveló que la unión de la carga induce la dimerización del Myosin VI CBD.

Conclusiones:

  • La dimerización inducida por la unión de carga es un mecanismo clave que regula la actividad y la procesividad de la miosina VI.
  • Este paradigma de dimerización puede extenderse a otras miosinas, como la Miosina VII y la Miosina X.