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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...
Anaphase A and B01:39

Anaphase A and B

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.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

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...
Microtubules in Cell Motility01:24

Microtubules in Cell Motility

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...
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,...
Destabilization of Microtubules01:45

Destabilization of Microtubules

The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...

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Related Experiment Video

Updated: May 18, 2026

Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
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Structural basis for microtubule binding and release by dynein.

W B Redwine1,2, R Hernandez-Lopez1, S Zou2

  • 1Department of Molecular and Cellular Biology, Harvard University, 52 Oxford Street, Cambridge, MA 02138, United States.

Science (New York, N.Y.)
|September 22, 2012
PubMed
Summary

Cytoplasmic dynein, a motor protein, uses microtubule binding and nucleotide hydrolysis for movement. New structural data reveals how microtubule interactions tune dynein

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Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
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Area of Science:

  • Molecular biology
  • Cell biology
  • Biophysics

Background:

  • Cytoplasmic dynein is a crucial microtubule-based motor protein.
  • It drives intracellular transport and cell division through cycles of track binding and nucleotide hydrolysis.
  • The mechanism linking microtubule binding to nucleotide hydrolysis across dynein's structure remains unclear.

Purpose of the Study:

  • To elucidate the structural basis of how dynein binds to microtubules.
  • To understand how microtubule binding is communicated to dynein's nucleotide-binding sites.
  • To reveal the molecular mechanisms tuning dynein's microtubule affinity.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine high-resolution structures.
  • Generation of a pseudo-atomic model using molecular dynamics simulations.
  • Mutagenesis studies and single-molecule motility assays for functional validation.

Main Results:

  • Subnanometer-resolution structure of dynein's microtubule-binding domain complexed with microtubules.
  • Identification of large structural rearrangements upon microtubule binding.
  • Mutagenesis and motility assays confirmed specific interactions that tune microtubule affinity.

Conclusions:

  • A molecular model for dynein-microtubule interaction and communication within the motor.
  • Insights into how dynein's track binding influences its motor activity.
  • Understanding the structural basis for regulating dynein's affinity to microtubules.