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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

Insights

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.

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.

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