Targeted gene disruption of dynein heavy chain 7 of<i>Tetrahymena thermophila</i>results in altered ciliary waveform and reduced swim speed

Wood, Christopher R.; Hard, R; Hennessey, Todd M.

doi:10.1242/jcs.007369

Cited by 41 publications

(29 citation statements)

References 35 publications

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“…Our results show that loss of ccp5 induces hyperglutamylation in zebrafish pronephric cilia and reduces cilia beat coordination and beat amplitude without affecting beat frequency. This may reflect a preferential effect of hyperglutamylation on inner dynein arm activity, consistent with previously reported effects of TTLL deficiency on axonemal microtubule sliding and the role of inner dynein arms in regulating cilia waveform (Brokaw and Kamiya, 1987; Wood et al. , 2007; Suryavanshi et al.…”

Section: Discussionsupporting

confidence: 90%

Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function

Pathak

Austin‐Tse

Liu

et al. 2014

MBoC

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Section: Discussionsupporting

confidence: 90%

Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function

Pathak

Austin‐Tse

Liu

et al. 2014

MBoC

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“…In the spermatozoa from mice lacking the inner arm dynein heavy chain 7 (DyHC7) gene, the lateral amplitude of the flagella beat is decreased by 50% compared with controls, resulting in reduced swimming velocities of spermatozoa, but their CBF was unaffected [28]. In Tetrahymena, DyHC6-or 7-knockout mutants show an irregular ciliary beat waveform, a normal CBF, and decreased swim speeds [19][20][21]. Thus, the results of this study are consistent with those previously reported in PCD patients, mice and Tetrahymena with inner arm dynein defects: that is, that an increase in CBA is the key factor controlling the rate of ciliary transport.…”

Section: Discussionmentioning

confidence: 99%

“…In transgenic mice that lack the inner arm dynein heavy chain 7 gene (DyHC7), spermatozoa flagella show an abnormal beating waveform and a decreased lateral amplitude but have a normal CBF. Chlamydomonas and Tetrahymena mutants lacking DyHC7 also show an irregular ciliary waveform pattern, decreased CBA, slower swim speed, but they still have a normal CBF [19,21,22]. These observations suggest that CBA is of particular importance for regulating the mucociliary transport rate in airways.…”

Section: Introductionmentioning

confidence: 89%

Procaterol-stimulated Increases in Ciliary Bend Amplitude and Ciliary Beat Frequency in Mouse Bronchioles

Komatani-Tamiya

Daikoku²,

Takemura³

et al. 2012

Cell Physiol Biochem

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The beating cilia play a key role in lung mucociliary transport. The ciliary beating frequency (CBF) and ciliary bend amplitude (CBA) of isolated mouse bronchiolar ciliary cells were measured using a light microscope equipped with a high-speed camera (500 Hz). Procaterol (aβ ₂-agonist) increased CBA and CBF in a dose dependent manner via cAMP. The time course of CBA increase is distinct from that of CBF increase: procaterol at 10 nM first increased CBA and then CBF. Moreover, 10 pM procaterol increased CBA, not CBF, whereas 10 nM procaterol increased both CBA and CBF. Concentration-response studies of procaterol demonstrated that the CBA curve was shifted to a lower concentration than the CBF curve, which suggests that CBA regulation is different from CBF regulation. Measurements of microbead movements on the bronchiole of lung slices revealed that 10 pM procaterol increased the rate of ciliary transport by 37% and 10 nM procaterol increased it by 70%. In conclusion, we have shown that increased CBA is of particular importance for increasing the bronchiolar ciliary transport rate, although CBF also plays a role in increasing it.

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“…The doublet is very stable and robust. It does not break under significant stress during rapid ciliary/flagellar beating with a frequency range of between ∼16 to 70 Hz1314. The outstanding stability of the doublet is likely linked to microtubule inner proteins (MIPs), which bind firmly to the inner wall of the doublet microtubule101115.…”

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confidence: 99%

Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

et al. 2017

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Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign α- and β-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule.

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Targeted gene disruption of dynein heavy chain 7 ofTetrahymena thermophilaresults in altered ciliary waveform and reduced swim speed

Abstract: SummaryTargeted gene disruption of dynein heavy chain 7 of Tetrahymena thermophila results in altered ciliary waveform and reduced swim speed

Cited by 41 publications

References 35 publications

Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function

Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function

Procaterol-stimulated Increases in Ciliary Bend Amplitude and Ciliary Beat Frequency in Mouse Bronchioles

Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins

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