Proteins of the Ciliary Axoneme Are Found on Cytoplasmic Membrane Vesicles during Growth of Cilia

Wood, Christopher R.; Rosenbaum, Joel L.

doi:10.1016/j.cub.2014.03.047

Cited by 46 publications

(46 citation statements)

References 32 publications

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“…Membrane trafficking plays an important role in the formation and function of cilia [9, 41, 44-48] and the ESCRT machinery may be a previously unrecognized component involved in the dynamics of the ciliary membrane. Identification of ESCRT proteins associated with the TZ of Chlamydomonas , along with other proteins identified in the TZ proteome, provides new clues to the functions of cilia and their involvement in ciliopathies.…”

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Isolated Ciliary Transition Zones Reveals the Presence of ESCRT Proteins

2015

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Summary The transition zone (TZ) is a specialized region of the cilium characterized by Y-shaped connectors between the microtubules of the ciliary axoneme and the ciliary membrane [1]. Located near the base of the cilium (Fig. 1A), the TZ is in the prime location to act as a gate for proteins into and out of the ciliary compartment, a role supported by experimental evidence [2-6]. The importance of the TZ has been underscored by studies showing that mutations affecting proteins located in the TZ result in cilia-related diseases, or ciliopathies, presenting symptoms including renal cysts, retinal degeneration, and situs inversus [7-9]. Some TZ proteins have been identified and shown to interact with each other through coprecipitation studies in vertebrate cells [4, 10, 11] and genetics studies in C. elegans [3]. As a distinct approach to identify TZ proteins we have taken advantage of the biology of Chlamydomonas to isolate TZs. Proteomic analysis identified 115 proteins, 10 of which were known TZ proteins related to ciliopathies, indicating that the preparation was highly enriched for TZs. Interestingly, six proteins of the endosomal sorting complexes required for transport (ESCRT) were also associated with the TZs. Identification of these and other proteins in the TZ will provide new insights into functions of the TZ as well as candidate ciliopathy genes.

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Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Isolated Ciliary Transition Zones Reveals the Presence of ESCRT Proteins

2015

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“…It is also known that some IFT46 associates with cytoplasmic vesicles and is then delivered to the basal body region in C. reinhardtii (Wood and Rosenbaum, 2014). However, there are still two possibilities regarding the molecular mechanism of the basal body targeting of IFT46.…”

Section: Nls-tagged Ift52c Recruits Ift46 To Nucleimentioning

confidence: 91%

“…8). During flagellar regeneration in Chlamydomonas, IFT46 has been observed in TGN-derived vesicles (Wood and Rosenbaum, 2014), and it is possible that IFT52 and IFT46 are preassembled in the TGN and are delivered to the basal body through vesicular transport (Fig. 8).…”

Section: Discussionmentioning

confidence: 99%

“…However, the mechanism of the basal body localization of IFT subunits, which is one of the key steps in the initiation of ciliogenesis, remains largely unknown. Since the the IFT proteins, such as IFT46, are localized in trans-Golgi network (TGN)-derived vesicles during flagellar regeneration, Woods et al have suggested that IFT complexes may associate with the vesicle first, recruit the cargos, and then be targeted to the basal body (Wood and Rosenbaum, 2014). Many ciliary proteins, especially ciliary membrane proteins, contain ciliary-targeting sequences (CTSs) (Bhogaraju et al, 2013;Malicki and Avidor-Reiss, 2014).…”

Section: Introductionmentioning

confidence: 99%

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

Wan

Täschner

et al. 2017

Journal of Cell Science

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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.

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“…IFT particles continuously cycling between the cytoplasm and the flagellar compartment are first gathered in a pool at the flagellar base, where they associate with the basal body transitional fibres (Deane et al, 2001;Wei et al, 2013;Wood and Rosenbaum, 2014); from this pool, groups of particles organize into linear arrays -the IFT trains -and periodically enter the flagellum (Dentler, 2005;Ludington et al, 2013). The molecular mechanisms controlling the transit of particles through the transition zone and their organization into trains are largely unknown; similarly, very little is known about the molecular process controlling the reorganization of anterogrademoving trains into those moving in a retrograde manner at the tip, although, in Chlamydomonas, CDPK-1 has been recently implicated in kinesin-II inactivation and dissociation from the IFT-B subcomplex (Liang et al, 2014).…”

Section: Discussion Short Ift Trains Are Involved In Anterograde Tranmentioning

confidence: 99%

Two classes of short intraflagellar transport train with different 3D structures are present in Chlamydomonas flagella

Vannuccini

Paccagnini

Cantele

et al. 2016

Journal of Cell Science

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Intraflagellar transport (IFT) is responsible for the bidirectional trafficking of molecular components required for the elongation and maintenance of eukaryotic cilia and flagella. Cargo is transported by IFT 'trains', linear rows of multiprotein particles moved by molecular motors along the axonemal doublets. We have previously described two structurally distinct categories of 'long' and 'short' trains. Here, we analyse the relative number of these trains throughout flagellar regeneration and show that long trains are most abundant at the beginning of flagellar growth whereas short trains gradually increase in number as flagella elongate. These observations are incompatible with the previous hypothesis that short trains are derived solely from the reorganization of long trains at the flagellar tip. We demonstrate with electron tomography the existence of two distinct ultrastructural organizations for the short trains, we name these 'narrow' and 'wide', and provide the first 3D model of the narrow short trains. These trains are characterized by tri-lobed units, which repeat longitudinally every 16 nm and contact protofilament 7 of the B-tubule. Functional implications of the new structural evidence are discussed.

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Proteins of the Ciliary Axoneme Are Found on Cytoplasmic Membrane Vesicles during Growth of Cilia

Cited by 46 publications

References 32 publications

Proteomic Analysis of Isolated Ciliary Transition Zones Reveals the Presence of ESCRT Proteins

Proteomic Analysis of Isolated Ciliary Transition Zones Reveals the Presence of ESCRT Proteins

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

Two classes of short intraflagellar transport train with different 3D structures are present in Chlamydomonas flagella

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