From the cytoplasm into the cilium: Bon voyage

Malicki, Jarema; Avidor‐Reiss, Tomer

doi:10.4161/org.29055

Cited by 75 publications

(77 citation statements)

References 199 publications

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“…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). These CTSs mediate the basal body and ciliary localization of target proteins.…”

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

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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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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

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“…In particular, some ciliopathy patients display a range of neurological disorders including cognitive deficits (Lee and Gleeson, 2011), thereby highlighting the importance of primary cilia function within the brain (Green and Mykytyn, 2010). Let us briefly describe some main structural features of these crucial appendages and then some of their possible functional implications, while for a more detailed description, the reader is referred to several excellent reviews that have been recently published (Louvi and Grove, 2011;Guemez-Gamboa et al, 2014;Malicki and Avidor-Reiss, 2014). The primary cilium is about 1-5 microns in length and only 200-300 nm in diameter and consists of a ciliary membrane that surrounds an axoneme, composed of nine microtubule pairs (the 9+0 configuration) anchored to a microtubule organizer, the ciliary basal body (Louvi and Grove, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…The limiting factor is mainly the steric hindrance; hence, proteins > 9 nm in diameter are restricted from entering the cilia. Furthermore, it has been shown that cilia proteins can have specialized sequences, the ciliary targeting sequences, which direct the proteins to the ciliary compartment (Malicki and Avidor-Reiss, 2014). Thus, the primary cilium is a sensing organelle functionally separated from the cytoplasm by the ciliary base, which controls the selective entry of ciliary proteins (Wei et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

The multi-facet aspects of cell sentience and their relevance for the integrative brain actions: role of membrane protein energy landscape

Agnati¹,

Marcoli

Maura

et al. 2016

Reviews in the Neurosciences

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AbstractSeveral ion channels can be randomly and spontaneously in an open state, allowing the exchange of ion fluxes between extracellular and intracellular environments. We propose that the random changes in the state of ion channels could be also due to proteins exploring their energy landscapes. Indeed, proteins can modify their steric conformation under the effects of the physicochemical parameters of the environments with which they are in contact, namely, the extracellular, intramembrane and intracellular environments. In particular, it is proposed that the random walk of proteins in their energy landscape is towards attractors that can favor the open or close condition of the ion channels and/or intrinsic activity of G-protein-coupled receptors. The main aspect of the present proposal is that some relevant physicochemical parameters of the environments (e.g. molecular composition, temperature, electrical fields) with which some signaling-involved plasma membrane proteins are in contact alter their conformations. In turn, these changes can modify their information handling via a modulatory action on their random walk towards suitable attractors of their energy landscape. Thus, spontaneous and/or signal-triggered electrical activities of neurons occur that can have emergent properties capable of influencing the integrative actions of brain networks. Against this background, Cook’s hypothesis on ‘cell sentience’ is developed by proposing that physicochemical parameters of the environments with which the plasma-membrane proteins of complex cellular networks are in contact fulfill a fundamental role in their spontaneous and/or signal-triggered activity. Furthermore, it is proposed that a specialized organelle, the primary cilium, which is present in most cells (also neurons and astrocytes), could be of peculiar importance to pick up chemical signals such as ions and transmitters and to detect physical signals such as pressure waves, thermal gradients, and local field potentials.

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“…The dendrite of many of these neurons is composed of two parts: the inner segment and the sensory cilium (Keil 1997;Swaroop et al 2010) ( Figure 1A). The sensory cilium is composed of a connecting cilium, which is a specialized ciliary transition zone (Malicki and Avidor-Reiss 2014), and an outer segment, which houses the sensory transduction machinery . The main body of the dendrite, referred to as the inner segment, serves as a link between the neuronal cell body and the sensory cilium.…”

mentioning

confidence: 99%

“…Second, mutations affecting the connecting cilium, such as cep290 (den Hollander et al 2006;Cideciyan et al 2007;Basiri et al 2014), and sensory cilium, such as intraflagellar transport (IFT) proteins, have a similar effect in both human photoreceptor and Drosophila sensory function (Avidor-Reiss et al 2004;Crouse et al 2014). Third, the connecting cilium of both D. melanogaster mechanosensory neurons and human photoreceptors is uniquely long and serves as the connection between two bulky compartments: the inner and outer segments, which display much greater width and volume compared to the transition zone itself (Malicki and Avidor-Reiss 2014). This is likely to impose unusual structural requirements.…”

mentioning

confidence: 99%

Drosophila Hook-Related Protein (Girdin) Is Essential for Sensory Dendrite Formation

Polyanovsky

Avidor‐Reiss

2015

Genetics

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The dendrite of the sensory neuron is surrounded by support cells and is composed of two specialized compartments: the inner segment and the sensory cilium. How the sensory dendrite is formed and maintained is not well understood. Hook-related proteins (HkRP) like Girdin, DAPLE, and Gipie are actin-binding proteins, implicated in actin organization and in cell motility. Here, we show that the Drosophila melanogaster single member of the Hook-related protein family, Girdin, is essential for sensory dendrite formation and function. Mutations in girdin were identified during a screen for fly mutants with no mechanosensory function. Physiological, morphological, and ultrastructural studies of girdin mutant flies indicate that the mechanosensory neurons innervating external sensory organs (bristles) initially form a ciliated dendrite that degenerates shortly after, followed by the clustering of their cell bodies. Importantly, we observed that Girdin is expressed transiently during dendrite morphogenesis in three previously unidentified actin-based structures surrounding the inner segment tip and the sensory cilium. These actin structures are largely missing in girdin mutant. Defects in cilia are observed in other sensory organs such as those mediating olfaction and taste, suggesting that Girdin has a general role in forming sensory dendrites in Drosophila. These suggest that Girdin functions temporarily within the sensory organ and that this function is essential for the formation of the sensory dendrites via actin structures.

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From the cytoplasm into the cilium: Bon voyage

Cited by 75 publications

References 199 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

The multi-facet aspects of cell sentience and their relevance for the integrative brain actions: role of membrane protein energy landscape

Drosophila Hook-Related Protein (Girdin) Is Essential for Sensory Dendrite Formation

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