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Related Concept Videos

Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

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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...
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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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Microtubules are thick hollow cylindrical proteins that help form the cytoskeleton. Microtubules have varied roles in the cell. These filaments help form cellular appendages like cilia and flagella, which are responsible for locomotion. The cilia arise from basal bodies, separated from the main body by a membrane-like structure forming the transition zone. This zone is the gate for the entry of lipids and proteins, creating a unique composition of lipids and proteins in the ciliary membrane and...
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Assembly of Cytoskeletal Filaments01:18

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Anaphase A and B01:39

Anaphase A and B

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Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
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Assembly of Complex Microtubule Structures

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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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Related Experiment Video

Updated: Jan 13, 2026

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
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Subunit organization in cytoplasmic dynein subcomplexes.

Stephen J King1, Myriam Bonilla, Michael E Rodgers

  • 1Department of Biology, The Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA.

Protein Science : a Publication of the Protein Society
|April 23, 2002
PubMed
Summary

Cytoplasmic dynein

Area of Science:

  • Cell Biology
  • Molecular Motors
  • Protein Biochemistry

Background:

  • Cytoplasmic dynein is crucial for eukaryotic cell functions.
  • Understanding dynein's subunit organization is vital but challenging due to heterogeneity.
  • Heavy chains associate with intermediate, light intermediate, and light chains.

Purpose of the Study:

  • To investigate the organization of cytoplasmic dynein subunits.
  • To explore the assembly and compositional heterogeneity of dynein.
  • To understand how different intermediate chain isoforms bind light chains.

Main Methods:

  • Separation of cytoplasmic dynein into two distinct subcomplexes.
  • Reassembly of subcomplexes into dynein-like molecules.
  • Analytical velocity sedimentation of intermediate and light chain subcomplexes.

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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
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Production of Dynein and Kinesin Motor Ensembles on DNA Origami Nanostructures for Single Molecule Observation
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Main Results:

  • Identified two primary subcomplexes: heavy/light intermediate chains and intermediate/light chains.
  • The intermediate/light chain subcomplex separated into pools with distinct intermediate chain compositions.
  • Analytical velocity sedimentation revealed four molecular components related to intermediate and light chains.

Conclusions:

  • Dynein intermediate chain isoforms exhibit differential light chain-binding properties.
  • Cytoplasmic dynein exhibits significant compositional heterogeneity in vivo.
  • These findings offer new insights into dynein complex assembly and organization.