Intraflagellar transport trains and motors: Insights from structure

Webb, Stephanie; Mukhopadhyay, Aakash Gautam; Roberts, A. J.

doi:10.1016/j.semcdb.2020.05.021

Cited by 59 publications

(69 citation statements)

References 152 publications

(268 reference statements)

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“…IFT-A consists of both "core" and "peripheral" subunits, and IFT-B is known to consist of two sub-complexes, IFT-B1 and IFT-B2 (Behal et al, 2012;Cole et al, 1998;Katoh et al, 2016;Lucker et al, 2005;Lucker et al, 2010;Mukhopadhyay et al, 2010;Piperno and Mead, 1997;Taschner et al, 2011;. At the basal body, these subunits, along with IFT motors, assemble into higher-order structures called trains (Jordan et al, 2018;Webb et al, 2020). Whether subcomplexes share basal body recruitment and retention mechanisms remains unclear.…”

Section: Introductionmentioning

confidence: 99%

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Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Hibbard

Vazquez

Satija

et al. 2021

MBoC

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Intraflagellar transport (IFT) is essential for construction and maintenance of cilia. IFT proteins concentrate at the basal body, where they are thought to assemble into trains and bind cargoes for transport. To study the mechanisms of IFT recruitment to this peri-basal body pool, we quantified protein dynamics of eight IFT proteins, as well as five other basal body localizing proteins, using fluorescence recovery after photobleaching in vertebrate multiciliated cells. We found that members of the IFT-A and IFT-B protein complexes show distinct turnover kinetics from other basal body components. Additionally, known IFT sub-complexes displayed shared dynamics, suggesting shared basal body recruitment and/or retention mechanisms. Finally, we evaluated the mechanisms of basal body recruitment by depolymerizing cytosolic MTs, which suggested that IFT proteins are recruited to basal bodies through a diffusion-to-capture mechanism. Our survey of IFT protein dynamics provides new insights into IFT recruitment to basal bodies, a crucial step in ciliogenesis and ciliary signaling.

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Section: Introductionmentioning

confidence: 99%

“…At the basal body, these subunits, along with IFT motors, assemble into higher-order structures called trains ( Jordan et al. , 2018 ; Webb et al. , 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Hibbard

Vazquez

Satija

et al. 2021

MBoC

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“…IFT-A consists of both “core” and “peripheral” sub-units, and IFT-B is known to consist of two sub-complexes, IFT-B1 and IFT-B2 (Behal et al, 2012; Cole et al, 1998; Katoh et al, 2016; Lucker et al, 2005; Lucker et al, 2010; Mukhopadhyay et al, 2010; Piperno and Mead, 1997; Taschner et al, 2011; Taschner et al, 2016). At the basal body, these subunits, along with IFT motors, assemble into higher-order structures called trains (Webb et al, 2020). Whether subcomplexes share basal body recruitment and retention mechanisms remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Protein turnover dynamics suggest a diffusion to capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Hibbard

Vazquez

Satija³

et al. 2020

Preprint

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Intraflagellar transport (IFT) is essential for construction and maintenance of cilia. IFT proteins concentrate at the basal body, where they are thought to assemble into trains and bind cargoes for transport. To study the mechanisms of IFT recruitment to this peri-basal body pool, we quantified protein dynamics of eight IFT proteins, as well as five other basal body localizing proteins, using fluorescence recovery after photobleaching in vertebrate multiciliated cells. We found that members of the IFT-A and IFT-B protein complexes show distinct turnover kinetics from other basal body components. Additionally, known IFT sub-complexes displayed shared dynamics, and these dynamics were not altered during cilia regeneration as compared to homeostasis. Finally, we evaluated the mechanisms of basal body recruitment by depolymerizing cytosolic MTs, which suggested that IFT proteins are recruited to basal bodies through a diffusion-to-capture mechanism. Our survey of IFT protein dynamics provides new insights into IFT recruitment to basal bodies, a crucial step in ciliogenesis.

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“…IFT is mediated by large complexes of proteins that form “IFT trains” which can move in either direction along the cilium. Two classes of IFT have been characterized; IFT-A moves in the retrograde direction, from cilium tip to base, utilizing dynein motors, whereas IFT-B moves in the anterograde direction via kinesin motors (Scholey, 2013 ; Lechtreck, 2015 ; Reilly and Benmerah, 2019 ; Webb et al, 2020 ). The IFT complex itself is a super-molecular structure that possesses both IFT-A and IFT-B components working together in ciliary protein import and export (Kobayashi et al, 2020 ).…”

Section: Intraflagellar Transport In Photoreceptorsmentioning

confidence: 99%

Compartmentalization of Photoreceptor Sensory Cilia

Barnes

Malhotra

Calvert

2021

Front. Cell Dev. Biol.

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Functional compartmentalization of cells is a universal strategy for segregating processes that require specific components, undergo regulation by modulating concentrations of those components, or that would be detrimental to other processes. Primary cilia are hair-like organelles that project from the apical plasma membranes of epithelial cells where they serve as exclusive compartments for sensing physical and chemical signals in the environment. As such, molecules involved in signal transduction are enriched within cilia and regulating their ciliary concentrations allows adaptation to the environmental stimuli. The highly efficient organization of primary cilia has been co-opted by major sensory neurons, olfactory cells and the photoreceptor neurons that underlie vision. The mechanisms underlying compartmentalization of cilia are an area of intense current research. Recent findings have revealed similarities and differences in molecular mechanisms of ciliary protein enrichment and its regulation among primary cilia and sensory cilia. Here we discuss the physiological demands on photoreceptors that have driven their evolution into neurons that rely on a highly specialized cilium for signaling changes in light intensity. We explore what is known and what is not known about how that specialization appears to have driven unique mechanisms for photoreceptor protein and membrane compartmentalization.

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Intraflagellar transport trains and motors: Insights from structure

Cited by 59 publications

References 152 publications

Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Protein turnover dynamics suggest a diffusion-to-capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Protein turnover dynamics suggest a diffusion to capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins

Compartmentalization of Photoreceptor Sensory Cilia

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