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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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Role of Septins01:02

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Septins are the recently discovered fourth major protein component of the cytoskeleton, along with microfilaments, microtubules, and intermediate filaments. These proteins can associate with other cytoskeletal filaments and carry out varied roles or can be free-floating in the cytoplasm.
Cellular Functions of Septins
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The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
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Microtubules in Cell Motility01:24

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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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The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

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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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Spindle Assembly02:50

Spindle Assembly

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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Updated: Jun 29, 2025

Reconstitution of Basic Mitotic Spindles in Spherical Emulsion Droplets
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Roles for CEP170 in cilia function and dynein-2 assembly.

Johannes F Weijman1, Laura Vuolo1, Caroline Shak1

  • 1Cell Biology Laboratories, School of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, UK.

Journal of Cell Science
|March 27, 2024
PubMed
Summary
This summary is machine-generated.

Centrosomal protein 170 (CEP170) is crucial for primary cilia function. It interacts with dynein-2, a motor protein complex essential for intraflagellar transport, aiding in dynein-2 assembly and stability.

Keywords:
CEP170CentrosomeCiliaDynein-2Intraflagellar transportMicrotubule motors

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Organelle Biology

Background:

  • Primary cilia are vital eukaryotic organelles involved in cellular signaling and secretion.
  • Dynein-2, a motor protein complex, is essential for ciliogenesis through retrograde intraflagellar transport (IFT).
  • The assembly and recycling mechanisms of dynein-2 within cilia remain largely unknown.

Purpose of the Study:

  • To identify novel proteins involved in dynein-2 assembly and function.
  • To elucidate the role of centrosomal protein of 170 kDa (CEP170) in cilia biology.
  • To understand how CEP170 influences intraflagellar transport and dynein-2 complex stability.

Main Methods:

  • Co-immunoprecipitation to identify dynein-2 interacting proteins.
  • siRNA-mediated knockdown of CEP170 in mammalian cells.
  • Analysis of intraflagellar transport dynamics and hedgehog signaling.
  • Assessment of dynein-2 holoenzyme complex stability.

Main Results:

  • CEP170 was identified as a novel dynein-2 interacting protein.
  • Loss of CEP170 disrupted intraflagellar transport and hedgehog signaling pathways.
  • CEP170 depletion affected the stability of the dynein-2 holoenzyme complex.
  • CEP170 is localized to the centrosome and interacts with dynein-2.

Conclusions:

  • CEP170 plays a significant role in supporting primary cilia function.
  • CEP170 is involved in the proper assembly and stability of the dynein-2 motor complex.
  • CEP170 is a key regulator of retrograde intraflagellar transport.