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Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity
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 poc1∆ cells, electron tomography reveals subtle defects in the organization of in...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966981/ https://www.ncbi.nlm.nih.gov/pubmed/27251062 http://dx.doi.org/10.1091/mbc.E16-03-0165 |
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author | Meehl, Janet B. Bayless, Brian A. Giddings, Thomas H. Pearson, Chad G. Winey, Mark |
author_facet | Meehl, Janet B. Bayless, Brian A. Giddings, Thomas H. Pearson, Chad G. Winey, Mark |
author_sort | Meehl, Janet B. |
collection | PubMed |
description | 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 poc1∆ 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. |
format | Online Article Text |
id | pubmed-4966981 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-49669812016-10-16 Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity Meehl, Janet B. Bayless, Brian A. Giddings, Thomas H. Pearson, Chad G. Winey, Mark Mol Biol Cell Articles 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 poc1∆ 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. The American Society for Cell Biology 2016-08-01 /pmc/articles/PMC4966981/ /pubmed/27251062 http://dx.doi.org/10.1091/mbc.E16-03-0165 Text en © 2016 Meehl et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Meehl, Janet B. Bayless, Brian A. Giddings, Thomas H. Pearson, Chad G. Winey, Mark Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title | Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title_full | Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title_fullStr | Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title_full_unstemmed | Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title_short | Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
title_sort | tetrahymena poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966981/ https://www.ncbi.nlm.nih.gov/pubmed/27251062 http://dx.doi.org/10.1091/mbc.E16-03-0165 |
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