Tetrahymena Poc1 ensures proper intertriplet microtubule linkages to maintain basal body integrity
| Autor: | Thomas H. Giddings, Janet B. Meehl, Mark Winey, Chad G. Pearson, Brian A. Bayless |
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| Přispěvatelé: | Doxsey, Stephen |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
congenital hereditary and neonatal diseases and abnormalities Electron Microscope Tomography Quantitative Biology::Tissues and Organs Protozoan Proteins macromolecular substances Medical and Health Sciences Microtubules Quantitative Biology::Subcellular Processes 03 medical and health sciences Microtubule medicine Basal body Cilia Ciliary beating Molecular Biology Cytoskeleton Centrioles Physics::Biological Physics biology Quantitative Biology::Neurons and Cognition Extramural Tetrahymena Cell Biology Articles Biological Sciences biology.organism_classification medicine.disease Basal Bodies Ciliopathies Cell biology Ciliopathy 030104 developmental biology Motile cilium Developmental Biology |
| Zdroj: | Molecular Biology of the Cell Molecular biology of the cell, vol 27, iss 15 |
| ISSN: | 1939-4586 1059-1524 |
| Popis: | The symmetric triplet microtubules of basal bodies resist asymmetric forces produced by motile cilia. The Poc1 basal body stability factor promotes the symmetric linkages between triplet microtubules. When Poc1 is absent, basal bodies exhibit the asymmetric loss of specific triplet microtubules. 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. |
| Databáze: | OpenAIRE |
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