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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 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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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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The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
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Dido3-dependent HDAC6 targeting controls cilium size.

Ainhoa Sánchez de Diego1, Astrid Alonso Guerrero1, Carlos Martínez-A1

  • 1Department of Immunology and Oncology, Centro Nacional de Biotecnología (CNB-CSIC), C/Darwin 3, Campus UAM Cantoblanco, 28049 Madrid, Spain.

Nature Communications
|March 27, 2014
PubMed
Summary

Death inducer obliterator (Dido3) and histone deacetylase 6 (HDAC6) control primary cilium size by regulating tubulin acetylation. Their localization, dependent on the actin network, determines cilium length in non-dividing cells.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Primary cilia are crucial for environmental sensing, cell growth, and development.
  • Defects in primary cilia are linked to various developmental disorders and pathologies.
  • Mechanisms regulating steady-state primary cilium size remain largely unknown.

Purpose of the Study:

  • To investigate the molecular mechanisms controlling primary cilium size in growth-arrested cells.
  • To identify key proteins and pathways that determine steady-state cilium length.

Main Methods:

  • Investigated the role of Dido3 and HDAC6 in primary cilia.
  • Analyzed protein localization using microscopy.
  • Assessed tubulin acetylation levels.
  • Examined the dependence on the actin network.

Main Results:

  • Dido3-dependent targeting of HDAC6 is a key determinant of cilium size.
  • The levels of Dido3 and HDAC6 negatively correlate with cilium size.
  • Dido3 availability at the centrosome controls ciliary HDAC6 levels and tubulin acetylation.
  • Basal body localization of Dido3 and HDAC6 depends on the actin network.

Conclusions:

  • Dido3 and HDAC6 regulate primary cilium size by controlling tubulin acetylation.
  • Subcellular distribution of HDAC6, in addition to its activity, influences substrate selection.
  • The actin network plays a role in regulating cilium size by controlling Dido3 and HDAC6 localization.