Electron-tomographic analysis of intraflagellar transport particle trains in situ

Pigino, Gaia; Geimer, Stefan; Lanzavecchia, Salvatore; Paccagnini, Eugenio; Cantele, Francesca; Diener, Dennis R.; Rosenbaum, Joel L.; Lupetti, Pietro

doi:10.1083/jcb.200905103

Cited by 191 publications

(240 citation statements)

References 47 publications

Supporting

Mentioning

213

Contrasting

Unclassified

Order By: Relevance

“…Anterograde IFT occurs over a distance of about 233 nm and moves along B-microtubules. Retrograde IFT occurs over a distance of about 209 nm and moves along A-microtubules (Pigino et al, 2009;Stepanek and Pigino, 2016). In addition, IFT proteins also function in other cellular processes, including vesicle exocytosis, cell division and the formation of immunological synapses and microtubule-based nanotubes (Baldari and Rosenbaum, 2010;Borovina and Ciruna, 2013;Griffiths et al, 2010;Inaba et al, 2015;Wood et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

“…Since cilia lack the machinery for protein synthesis, proteins -including structural components and signaling molecules -are synthesized in the cell body, and some are delivered into cilia via IFT. IFT and cargos may assemble into periodic IFT trains (Pigino et al, 2009;Stepanek and Pigino, 2016;Vannuccini et al, 2016). Anterograde IFT occurs over a distance of about 233 nm and moves along B-microtubules.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella

Wan

Täschner

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

Cilia are microtubule-based organelles and perform motile, sensing and signaling functions. The assembly and maintenance of cilia depend on intraflagellar transport (IFT). Besides ciliary localization, most IFT proteins accumulate at basal bodies. However, little is known about the molecular mechanism of basal body targeting of IFT proteins. We first identified the possible basal body-targeting sequence in IFT46 by expressing IFT46 truncation constructs in an ift46-1 mutant. The C-terminal sequence between residues 246-321, termed BBTS3, was sufficient to target YFP to basal bodies in the ift46-1 strain. Interestingly, BBTS3 is also responsible for the ciliary targeting of IFT46. BBTS3::YFP moves bidirectionally in flagella and interacts with other IFT complex B (IFT-B) proteins. Using IFT and motor mutants, we show that the basal body localization of IFT46 depends on IFT52, but not on IFT81, IFT88, IFT122, FLA10 or DHC1b. IFT52 interacts with IFT46 through residues L285 and L286 of IFT46 and recruits it to basal bodies. Ectopic expression of the C-terminal domain of IFT52 in the nucleus resulted in accumulation of IFT46 in nuclei. These data suggest that IFT52 and IFT46 can preassemble as a complex in the cytoplasm, which is then targeted to basal bodies.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella

Wan

Täschner

et al. 2017

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…The construction relies on an evolutionary conserved process called intraflagellar transport (IFT), a bi-directional movement of multiprotein complexes between the membrane and the axoneme microtubules (Kozminski et al, 1993). IFT particles or trains (Pigino et al, 2009) are composed of proteins that can be separated into a complex A and a complex B (Cole et al, 1998;Piperno and Mead, 1997). IFT proteins are found along the length of cilia (mature or in construction), but a substantial proportion is also found at the basal body area and in the cell body (Absalon et al, 2008;Cole et al, 1998;Deane et al, 2001;Pazour et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Fort

Bonnefoy

Kohl

et al. 2016

Journal of Cell Science

View full text Add to dashboard Cite

Intraflagellar transport (IFT) is required for construction of most cilia and flagella. Here, we used electron microscopy, immunofluorescence and live video microscopy to show that IFT is absent or arrested in the mature flagellum of Trypanosoma brucei upon RNA interference (RNAi)-mediated knockdown of IFT88 and IFT140, respectively. Flagella assembled prior to RNAi did not shorten, showing that IFT is not essential for the maintenance of flagella length. Although the ultrastructure of the axoneme was not visibly affected, flagellar beating was strongly reduced and the distribution of several flagellar components was drastically modified. The R subunit of the protein kinase A was no longer concentrated in the flagellum but was largely found in the cell body whereas the kinesin 9B motor was accumulating at the distal tip of the flagellum. In contrast, the distal tip protein FLAM8 was dispersed along the flagellum. This reveals that IFT also functions in maintaining the distribution of some flagellar proteins after construction of the organelle is completed.

show abstract

“…Structural analysis of IFT has not progressed rapidly but elegant high resolution EM tomographic reconstructions of intact IFT particles reveal convoluted structures that bridge from the ciliary membrane to the axonemal microtubules (50). To complement this top-down approach, other studies have focused on specific interactions within the IFT motors and complexes.…”

mentioning

confidence: 99%

Subunit Interactions and Organization of the Chlamydomonas reinhardtii Intraflagellar Transport Complex A Proteins

Behal

Miller

Qin

et al. 2012

Journal of Biological Chemistry

111

View full text Add to dashboard Cite

show abstract

Electron-tomographic analysis of intraflagellar transport particle trains in situ

Abstract: Ultrastructural study of Chlamydomonas cilia shows that anterograde IFT particles form trains that are long and narrow, while retrograde IFT form short, compact particle trains.

Cited by 191 publications

References 47 publications

Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella

Intraflagellar transport protein IFT52 recruits IFT46 to the basal body and flagella

Intraflagellar transport is required for the maintenance of the trypanosome flagellum composition but not its length

Subunit Interactions and Organization of the Chlamydomonas reinhardtii Intraflagellar Transport Complex A Proteins

Contact Info

Product

Resources

About