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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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Destabilization of Microtubules01:45

Destabilization of Microtubules

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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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Mechanism of Ciliary Motion01:05

Mechanism of Ciliary Motion

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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.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
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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.
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
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Actin Filament Depolymerization01:19

Actin Filament Depolymerization

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Related Experiment Video

Updated: Sep 1, 2025

Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends
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Preparation of Segmented Microtubules to Study Motions Driven by the Disassembling Microtubule Ends

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DYF-5/MAK-dependent phosphorylation promotes ciliary tubulin unloading.

Xuguang Jiang1, Wenxin Shao1, Yongping Chai1

  • 1Tsinghua-Peking Center for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences and Ministry of Education Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, China.

Proceedings of the National Academy of Sciences of the United States of America
|August 15, 2022
PubMed
Summary

Cilia formation relies on intraflagellar transport (IFT) to deliver tubulin. A novel kinase, DYF-5/MAK, controls tubulin unloading at ciliary tips by phosphorylating IFT-74, regulating cilia length.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Cilia are vital microtubule-based organelles involved in cell motility, sensation, and signaling.
  • Dysfunctional cilia lead to various human diseases known as ciliopathies.
  • Intraflagellar transport (IFT) is essential for cilia assembly and maintenance, utilizing motor proteins to move cargo.

Purpose of the Study:

  • To investigate the mechanism of tubulin unloading at the ciliary tip during ciliogenesis.
  • To identify the regulatory factors controlling tubulin release from IFT machinery.
  • To understand the role of ciliary kinases in ciliogenesis and cilia length regulation.

Main Methods:

  • Utilized *Caenorhabditis elegans* as a model organism.
  • Investigated the interaction between tubulin and the IFT-74/81 module.
  • Analyzed the effect of DYF-5/MAK kinase activity on IFT-74 phosphorylation and tubulin binding.
  • Assessed the impact of altered IFT-74 phosphorylation on sensory cilia length.

Main Results:

  • Identified DYF-5/MAK as a ciliary kinase that phosphorylates the tubulin-binding module of IFT-74.
  • Demonstrated that DYF-5/MAK phosphorylation reduces the affinity of IFT-74/81 for tubulin by approximately sixfold.
  • Showed that aberrant IFT-74 phosphorylation leads to abnormal sensory cilia elongation or shortening in *C. elegans* neurons.

Conclusions:

  • DYF-5/MAK-dependent phosphorylation of IFT-74 is crucial for regulating tubulin unloading at the ciliary tip.
  • This phosphorylation event plays a fundamental role in controlling ciliogenesis and maintaining proper cilia length.
  • The findings provide new insights into the molecular mechanisms governing cilia assembly and potential therapeutic targets for ciliopathies.