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Related Concept Videos

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.
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The primary cilium, made up of microtubules, acts as antennae on the cell surfaces for relaying external stimuli into the cells. These fine hair-like structures are present, generally one per cell. These are non-motile cilia in a 9+0 microtubules arrangement, where the central pair of microtubules are absent. The primary cilia arise from the basal body embedded in the cell membrane. Intraflagellar transport (IFT) carries requisite proteins from the cytoplasm to the cilium because the primary...
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Positioning the cell division plane is a critical step during development and cell differentiation, particularly during mitosis when the plane is essential for determining the size of the two daughter cells. The cell division plane is perpendicular to the plane of chromosome segregation, but different types of organisms have different cell division mechanisms to suit their morphology and function. 
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Catenins01:23

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Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
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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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Anaphase Promoting Complex00:50

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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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Evaluation of Planar-Cell-Polarity Phenotypes in Ciliopathy Mouse Mutant Cochlea
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Structure of the ciliogenesis-associated CPLANE complex.

Gerasimos Langousis1, Simone Cavadini1, Niels Boegholm2

  • 1Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.

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|April 15, 2022
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Summary

Cilia assembly defects cause human diseases. This study reveals the structure of key ciliogenesis proteins (CPLANE complex) and their lipid binding, offering new insights into ciliopathies.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Human Genetics

Background:

  • Cilia are crucial cellular structures involved in various biological processes.
  • Dysfunctional cilia lead to a range of human diseases known as ciliopathies.
  • Ciliogenesis and planar polarity effector (CPLANE) proteins, including Wdpcp, Inturned, and Fuzzy, are vital for cilia assembly but their structures and functions are poorly understood.

Purpose of the Study:

  • To elucidate the structural basis of the CPLANE protein complex.
  • To understand the molecular mechanisms underlying ciliogenesis.
  • To identify potential molecular rationales for ciliopathies caused by CPLANE dysfunction.

Main Methods:

  • X-ray crystallography to determine near-atomic resolution structures of human and mouse CPLANE complexes.
  • Biochemical assays to investigate the interaction of the CPLANE complex with phospholipids.
  • Analysis of a CPLANE ciliopathy mutant to assess its lipid-binding properties.

Main Results:

  • Mammalian Wdpcp, Inturned, and Fuzzy proteins form a stable complex.
  • The near-atomic structures of human and mouse CPLANE complexes, including one bound to Rsg1, were determined.
  • The crescent-shaped CPLANE complex binds phospholipids, such as phosphatidylinositol 3-phosphate, through multiple modules.
  • A CPLANE ciliopathy mutant displayed altered lipid binding.

Conclusions:

  • The study provides the first structural and functional insights into the CPLANE complex, essential for ciliogenesis.
  • The findings reveal phospholipid binding as a key function of the CPLANE complex.
  • Aberrant lipid binding by CPLANE mutants offers novel molecular explanations for ciliopathies.