Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity

Janet B. Meehl, Brian A. Bayless, Thomas H. Giddings, Chad G. Pearson, Mark Winey

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Basal bodies comprise nine symmetric triplet microtubules that anchor forces produced by the asymmetric beat pattern of motile cilia. The ciliopathy protein Poc1 stabilizes basal bodies through an unknown mechanism. In poc1Δ cells, electron tomography reveals subtle defects in the organization of intertriplet linkers (A-C linkers) that connect adjacent triplet microtubules. Complete triplet microtubules are lost preferentially near the posterior face of the basal body. Basal bodies that are missing triplets likely remain competent to assemble new basal bodies with nine triplet microtubules, suggesting that the mother basal body microtubule structure does not template the daughter. Our data indicate that Poc1 stabilizes basal body triplet microtubules through linkers between neighboring triplets. Without this stabilization, specific triplet microtubules within the basal body are more susceptible to loss, probably due to force distribution within the basal body during ciliary beating. This work provides insights into how the ciliopathy protein Poc1 maintains basal body integrity.

Original languageEnglish (US)
Pages (from-to)2394-2403
Number of pages10
JournalMolecular Biology of the Cell
Volume27
Issue number15
DOIs
StatePublished - Aug 1 2016
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity'. Together they form a unique fingerprint.

  • Cite this