Three-dimensional Organization of Basal Bodies from Wild-Type and δ-Tubulin Deletion Strains of<i>Chlamydomonas reinhardtii</i>

O’Toole, Eileen; Giddings, Thomas H.; McIntosh, J. Richard; Dutcher, Susan K.

doi:10.1091/mbc.e02-11-0755

Cited by 142 publications

(130 citation statements)

References 48 publications

Supporting

Mentioning

121

Contrasting

Order By: Relevance

“…3F, Fig. 4E) (CavalierSmith, 1974;O'Toole et al, 2003). The dot in the central hub might represent a fine filament in cross section because, in some median longitudinal sections of bbs, a fine filament was seen emanating from the central hub at the proximal end of the cartwheel (not shown).…”

Section: Basal Bodiesmentioning

confidence: 95%

“…This is illustrated by a recent study in which minor defects in the basal bodies of a Chlamydomonas δ-tubulin deletion mutant were detected using dual-axis electron tomography (O'Toole et al, 2003). We felt that a detailed high-resolution map integrating all structural components of the Chlamydomonas basal apparatus was needed and decided to reinvestigate its ultrastructure using serial ultrathin sections of isolated cytoskeletons.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The ultrastructure of theChlamydomonas reinhardtiibasal apparatus: identification of an early marker of radial asymmetry inherent in the basal body

Geimer

Melkonian

2004

Journal of Cell Science

135

193

View full text Add to dashboard Cite

The biflagellate unicellular green alga Chlamydomonas reinhardtii is a classic model organism for the analysis of flagella and their organizers, the basal bodies. In this cell, the two flagella-bearing basal bodies, along with two probasal bodies and an array of fibers and microtubules, form a complex organelle called the basal apparatus. The ultrastructure of the basal apparatus was analysed in detail by serial thin-section electron microscopy of isolated cytoskeletons and several newly discovered features are described, including a marker for the rotational asymmetry inherent in the basal bodies and probasal bodies. In addition, the complex three-dimensional basal apparatus ultrastructure is resolved and illustrated, including the attachment sites of all basal apparatus elements to specific microtubular triplets of the basal bodies and probasal bodies. These data will facilitate both the localization of novel basal apparatus proteins and the analysis of mutants and RNA interference cells with only subtle defects in basal apparatus ultrastructure. The early harbinger of radial asymmetry described here could play a crucial role during basal body maturation by orienting the asymmetric attachment of the various associated fibers and therefore might define the orientation of the basal bodies and, ultimately, the direction of flagellar beating.

show abstract

Section: Basal Bodiesmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

The ultrastructure of theChlamydomonas reinhardtiibasal apparatus: identification of an early marker of radial asymmetry inherent in the basal body

Geimer

Melkonian

2004

Journal of Cell Science

135

193

View full text Add to dashboard Cite

show abstract

“…The basal body is composed of nine triplet microtubules that are assembled into an elaborate barrel-like structure ( Figure 1C) (24). The basal body is also known as the centriole that when surrounded by a dense matrix, called the pericentriolar material, forms the centrosome and functions as a microtubule organizing center during mitotic division.…”

Section: Cilia and Cell-cycle Regulationmentioning

confidence: 99%

“…At the distal end of the basal body just before the start of the cilia axoneme are the terminal plate and transition fibers (Figure 1C) (24,31) (reviewed in reference [9]). Although little is known about the composition of these structures, they are thought to function as a gatekeeper to regulate protein entry into the cilium.…”

Section: Cilia Architecturementioning

confidence: 99%

Role of Primary Cilia in the Pathogenesis of Polycystic Kidney Disease

Yoder¹

2007

Journal of the American Society of Nephrology

261

223

View full text Add to dashboard Cite

Cysts in the kidney are among the most common inherited human pathologies, and recent research has uncovered that a defect in cilia-mediated signaling activity is a key factor that leads to cyst formation. The cilium is a microtubule-based organelle that is found on most cells in the mammalian body. Multiple proteins whose functions are disrupted in cystic diseases have now been localized to the cilium or at the basal body at the base of the cilium. Current data indicate that the cilium can function as a mechanosensor to detect fluid flow through the lumen of renal tubules. Flow-mediated deflection of the cilia axoneme induces an increase in intracellular calcium and alters gene expression. Alternatively, a recent finding has revealed that the intraflagellar transport 88/polaris protein, which is required for cilia assembly, has an additional role in regulating cell-cycle progression independent of its function in ciliogenesis. Further research directed at understanding the relationship between the cilium, cell-cycle, and cilia-mediated mechanosensation and signaling activity will hopefully provide important insights into the mechanisms of renal cyst pathogenesis and lead to better approaches for therapeutic intervention.

show abstract

“…Studies in Tetrahymena suggest that the terminal plate contains pores for the passage of IFT "trains" that deliver axonemal components to the distal tip of flagella (10). Striated transitional fibers radiate from the distal end of the basal body triplets to join the plasma membrane (11)(12)(13)(14), forming blades thought to create a physical barrier preventing vesicles from entering the ciliary lumen. Electron microscopy (EM) studies in Chlamydomonas suggest that the junction of the transitional fibers and the membrane provides a docking site for IFT particles (15).…”

mentioning

confidence: 99%

Cilium transition zone proteome reveals compartmentalization and differential dynamics of ciliopathy complexes

Dean

Moreira-Leite

Varga

et al. 2016

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

View full text Add to dashboard Cite

The transition zone (TZ) of eukaryotic cilia and flagella is a structural intermediate between the basal body and the axoneme that regulates ciliary traffic. Mutations in genes encoding TZ proteins (TZPs) cause human inherited diseases (ciliopathies). Here, we use the trypanosome to identify TZ components and localize them to TZ subdomains, showing that the Bardet-Biedl syndrome complex (BBSome) is more distal in the TZ than the Meckel syndrome (MKS) complex. Several of the TZPs identified here have human orthologs. Functional analysis shows essential roles for TZPs in motility, in building the axoneme central pair apparatus and in flagellum biogenesis. Analysis using RNAi and HaloTag fusion protein approaches reveals that most TZPs (including the MKS ciliopathy complex) show long-term stable association with the TZ, whereas the BBSome is dynamic. We propose that some Bardet-Biedl syndrome and MKS pleiotropy may be caused by mutations that impact TZP complex dynamics.transition zone | cilium/flagellum | BBSome | MKS/B9 complex | trypanosome C ilia, or flagella (the two terms are used here interchangeably), are multifunctional organelles that were present in the last common eukaryotic ancestor (1). Defects in cilia are responsible for pleiotropic human diseases (called ciliopathies) and their function is essential for pathogenesis in protozoan parasites (2, 3).During ciliogenesis, a microtubule organizing center called the "basal body" docks at the membrane. Basal bodies are built from nine microtubule triplets and two microtubules from each triplet extend to form a transition zone (TZ) and, ultimately, the axoneme. Thus, the TZ represents a structural junction between the basal body and the axoneme.As expected from its strategic position between the basal body and the axoneme, the TZ acts as a "ciliary gate" that controls ciliary composition and function (4). Many ciliopathies are caused by defects in complexes that associate with the TZ, including Meckel syndrome (MKS), Joubert syndrome and Bardet-Biedl syndrome (BBS). Studies using murine kidney epithelial cells and embryos suggest that the MKS complex demarcates the ciliary membrane by forming a diffusion barrier at the base of the cilium (5-7). On the other hand, the BBS complex (BBSome) is an adapter for intraflagellar transport (IFT) complexes that cross the TZ barrier to transport sensory proteins between the ciliary membrane and the cell body (8, 9).The TZ has distinctive structural features. At the proximal boundary of the TZ, where the basal body C tubule terminates, a "terminal plate" crosses the TZ. Studies in Tetrahymena suggest that the terminal plate contains pores for the passage of IFT "trains" that deliver axonemal components to the distal tip of flagella (10). Striated transitional fibers radiate from the distal end of the basal body triplets to join the plasma membrane (11-14), forming blades thought to create a physical barrier preventing vesicles from entering the ciliary lumen. Electron microscopy (EM) studies in Chlamydomonas suggest that...

show abstract

Three-dimensional Organization of Basal Bodies from Wild-Type and δ-Tubulin Deletion Strains ofChlamydomonas reinhardtii

Cited by 142 publications

References 48 publications

The ultrastructure of theChlamydomonas reinhardtiibasal apparatus: identification of an early marker of radial asymmetry inherent in the basal body

The ultrastructure of theChlamydomonas reinhardtiibasal apparatus: identification of an early marker of radial asymmetry inherent in the basal body

Role of Primary Cilia in the Pathogenesis of Polycystic Kidney Disease

Cilium transition zone proteome reveals compartmentalization and differential dynamics of ciliopathy complexes

Contact Info

Product

Resources

About