Ciliogenesis, Ciliary Function, and Selective Isolation

Stephens, R. E.

doi:10.1021/cb8000217

Cited by 11 publications

(12 citation statements)

References 23 publications

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“…Previous studies have identified homologs for many DMT proteins (10,(35)(36)(37)(38); here, we show that this evolutionary conservation continues on a structural level. One exception is the strikingly different partition wall between Chlamydomonas and sea urchin flagella.…”

Section: Discussionsupporting

confidence: 73%

“…Assembly of the axoneme begins with the polymerization of tubulin and other proteins to form the A-tubules, extending directly from the plus-ends of the basal body A-tubules (32)(33)(34). Assembly of the A-tubule is complex and involves the following components: (i) αβ-tubulin with and without posttranslational modifications (6); (ii) the ribbon proteins tektins, Rib43a, Rib72/Efhc1, and Efhc2 (35)(36)(37)(38); (iii) the structural components MIP1a/MIP1b and MIP2a/ MIP2b, for which the protein composition has not yet been identified (10); and (iv) possibly other unidentified proteins. It is not known whether all these various proteins coassemble with tubulin to form the A-tubule or are added later.…”

Section: Discussionmentioning

confidence: 99%

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Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Nicastro¹,

Heuser³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

136

208

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The axoneme forms the essential and conserved core of cilia and flagella. We have used cryo-electron tomography of Chlamydomonas and sea urchin flagella to answer long-standing questions and to provide information about the structure of axonemal doublet microtubules (DMTs). Solving an ongoing controversy, we show that B-tubules of DMTs contain exactly 10 protofilaments (PFs) and that the inner junction (IJ) and outer junction between the A-and B-tubules are fundamentally different. The outer junction, crucial for the initiation of doublet formation, appears to be formed by close interactions between the tubulin subunits of three PFs with unusual tubulin interfaces; other investigators have reported that this junction is weakened by mutations affecting posttranslational modifications of tubulin. The IJ consists of an axially periodic ladder-like structure connecting tubulin PFs of the A-and B-tubules. The recently discovered microtubule inner proteins (MIPs) on the inside of the A-and B-tubules are more complex than previously thought. They are composed of alternating small and large subunits with periodicities of 16 and/or 48 nm. MIP3 forms arches connecting B-tubule PFs, contrary to an earlier report that MIP3 forms the IJ. Finally, the "beak" structures within the B-tubules of Chlamydomonas DMT1, DMT5, and DMT6 are clearly composed of a longitudinal band of proteins repeating with a periodicity of 16 nm. These findings, discussed in relation to genetic and biochemical data, provide a critical foundation for future work on the molecular assembly and stability of the axoneme, as well as its function in motility and sensory transduction.microtubule stability | cilia | axoneme | ciliopathies | cytoskeleton

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Section: Discussionsupporting

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Nicastro¹,

Heuser³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

136

208

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“…These ∼50-kDa proteins have been characterized extensively from echinoderm and molluscan cilia (30, 32, 33, 35, 36, 51), and they have been identified in genomes ranging from protists to humans (27, 30). Tektins are expressed in mouse olfactory epithelial cells and photoreceptors that contain nonmotile, primary cilia (31), but they have not been found by proteomic studies of primary cilia of mouse kidney cells (52).…”

Section: Introductionmentioning

confidence: 99%

Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules

Linck

Lin

et al. 2014

Journal of Biological Chemistry

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Background: Ciliary microtubules contain hyperstable Ribbons of adjoining protofilaments.Results: Using echinoderm flagella, the locations of Ribbons, tektins, and Ca2+-binding proteins (related to human epilepsy) are studied biochemically and by immuno-cryo-electron tomography.Conclusion: The locations of these proteins create a biochemically, structurally unique region of ciliary A-microtubules.Significance: The results indicate specialized functions for Ribbons, with potential roles in assembly, motility, and/or signal transduction.

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“…The swimming of marine larvae depends on ciliary propulsion and is critically important for feeding, escape responses (Strathmann, 2007;Stephens, 2008) and photosensitive vertical migration (Ooka et al, 2010). In sea urchin embryos, motile cilia are evident from the blastula stage, and rotatory movement by embryos can be observed in the fertilization envelope.…”

Section: Introductionmentioning

confidence: 99%

“…Nevertheless, the swimming behavior of blastulae is organized to a considerable degree. For instance, sea urchin blastulae can swim by orienting their long apical tuft cilia in the target direction (Soliman, 1983a;Stephens, 2008). This suggests that swimming in sea urchin blastulae might be regulated by a distinctive mechanism that is not related to the 5HT-NS.…”

Section: Introductionmentioning

confidence: 99%

Development of a dopaminergic system in sea urchin embryos and larvae

Katow

Suyemitsu

Ooka

et al. 2010

Journal of Experimental Biology

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SUMMARYThe mechanisms that regulate the organized swimming movements of sea urchin blastulae are largely unknown. Using immunohistochemistry, we found that dopamine (DA) and the Hemicentrotus pulcherrimus homolog of the dopamine receptor D1 (Hp-DRD1) were strongly co-localized in 1-2m diameter granules (DA/DRD1 granules). Furthermore, these granules were arranged across the entire surface of blastulae as they developed locomotory cilia before hatching, and remained evident until metamorphosis. DA/DRD1 granules were associated with the basal bodies of cilia, and were densely packed in the ciliary band by the eight-arm pluteus stage. The transcription of Hp-DRD1 was detected from the unfertilized egg stage throughout the period of larval development. Treatment with S-(-)-carbidopa, an inhibitor of aromatic-L-amino acid decarboxylase, for 20-24h (i) from soon after insemination until the 20h post-fertilization (20hpf) early gastrula stage and (ii) from the 24hpf prism larva stage until the 48hpf pluteus stage, inhibited the formation of DA granules and decreased the swimming activity of blastulae and larvae in a dose-dependent manner. Exogenous DA rescued these deprivations. The formation of DRD1 granules was not affected. However, in 48hpf plutei, the serotonergic nervous system (5HT-NS) developed normally. Morpholino antisense oligonucleotides directed against Hp-DRD1 inhibited the formation of DRD1 granules and the swimming of larvae, but did not disturb the formation of DA granules. Thus, the formation of DRD1 granules and DA granules occurs chronologically closely but mechanically independently and the swimming of blastulae is regulated by the dopaminergic system. In plutei, the 5HT-NS closely surrounded the ciliary bands, suggesting the functional collaboration with the dopaminergic system in larvae. Supplementary material available online at

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Ciliogenesis, Ciliary Function, and Selective Isolation

Cited by 11 publications

References 23 publications

Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

Insights into the Structure and Function of Ciliary and Flagellar Doublet Microtubules

Development of a dopaminergic system in sea urchin embryos and larvae

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