Dynein and intraflagellar transport

Hou, Yuqing; Witman, George B.

doi:10.1016/j.yexcr.2015.02.017

Cited by 57 publications

(58 citation statements)

References 86 publications

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“…This conclusion is supported by a recent report that showed IFT dynein is required for transport of membrane proteins to the peri-basal body region in Chlamydomonas [43]. In mammalian cells, there are two types of cytoplasmic dynein: cytoplasmic dynein 1 and IFT dynein[52]. Interestingly, tandem affinity purification of IFT-A in mouse has identified cytoplasmic dynein 1 but not IFT dynein[17, 44], raising the possibility that cytoplasmic dynein 1 mediates IFT-A transport in the cell body of mammalian cells.…”

Section: Discussionsupporting

confidence: 56%

Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis

Zhu

Wang

et al. 2017

PLoS Genet

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Intraflagellar transport (IFT) particles or trains are composed of IFT-A and IFT-B complexes. To assess the working mechanism of the IFT-A complex in IFT and ciliogenesis, we have analyzed ift43 mutants of Chlamydomnonas in conjunction with mutants of the other IFT-A subunits. An ift43 null mutant or a mutant with a partial deletion of the IFT43 conserved domain has no or short flagella. The mutants accumulate not only IFT-B but also IFT-Ain the short flagella, which is in contrast to an ift140 null mutant. The IFT43 conserved domain is necessary and sufficient for the function of IFT43. IFT43 directly interacts with IFT121 and loss of IFT43 results in instability of IFT-A. A construct with a partial deletion of the IFT43 conserved domain is sufficient to rescue the instability phenotype of IFT-A, but results in diminishing of IFT-A at the peri-basal body region. We have further provided evidence for the direct interactions within the IFT-A complex and shown that the integrity of IFT-A is important for its stability and cellular localization. Finally, we show that both IFT43 and IFT140 are involved in mobilizing ciliary precursors from the cytoplasmic pool during flagellar regeneration, suggesting a novel role of IFT-A in transporting ciliary components in the cytoplasm to the peri-basal body region.

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Section: Discussionsupporting

confidence: 56%

Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis

Zhu

Wang

et al. 2017

PLoS Genet

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“…IFT is the process by which the cilium is assembled and maintained. It is powered by two conserved, dedicated microtubule motors: anterograde transport from the base to the tip depends on a plus-end directed heterotrimeric kinesin-2 complex, KIF3a, KIF3b and KIF associated protein 3 (KAP3) (Cole, 1999) and retrograde transport from the tip to the base requires the minus-end-directed cytoplasmic dynein2 motor made up of a heavy chain, an intermediate chain, light intermediate chain and several light chains (Hou and Witman, 2015). These motors are coupled to the cargos by large electron-dense IFT trains, made up of two protein complexes, IFT-A and IFT-B (Pigino et al 2009; Behal and Cole 2013).…”

Section: Intraflagellar Transport (Ift) Is Required For Shh Signal Trmentioning

confidence: 99%

Primary Cilia and Mammalian Hedgehog Signaling

Bangs

Anderson

2016

Cold Spring Harb Perspect Biol

513

489

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It has been a decade since it was discovered that primary cilia have an essential role in Hedgehog signaling in mammals. This discovery came from screens in the mouse that identified a set of genes that are required for both normal Hedgehog signaling and for the formation of primary cilia. Since then, dozens of mouse mutations have been identified that disrupt cilia in a variety of ways and have complex effects on Hedgehog signaling. Here we summarize the genetic and developmental studies used to deduce how Hedgehog signal transduction is linked to cilia and the complex effects that perturbation of cilia structure can have on Hh signaling. We conclude by describing the current status of our understanding of the cell-type specific regulation of ciliogenesis and how that determines the ability of cells to respond to Hedgehog ligands.

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“…The cytoplasmic dynein-2 heavy chain includes six C-terminal AAA+ domains required for ATP hydrolysis and motor activity, a linker domain for microtubule attachment, and an N-terminal region that mediates homodimerization and subsequent interaction with dynein regulatory subunits [63] (Figure 4). The seven accessory subunits are the dynein light chains, intermediate chains, and light intermediate chain [64]. …”

Section: Cytoplasmic Dynein-2: the Retrograde Ciliary Motormentioning

confidence: 99%

Microtubule Motors Drive Hedgehog Signaling in Primary Cilia

Agbu

Anderson

2017

Trends in Cell Biology

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The mammalian Hedgehog (Hh) signaling pathway is required for development and for maintenance of adult stem cells, and overactivation of the pathway can cause tumorigenesis. All responses to Hh family ligands in mammals require the primary cilium, an ancient microtubule-based organelle that extends from the cell surface. Genetic studies in mice and humans have defined specific functions for cilia-associated microtubule motor proteins: they act in the construction and disassembly of the primary cilium, they control cilia length and stability, and some have direct roles in mammalian Hh signal transduction. These studies highlight how integrated genetic and cell biological studies can define the molecular mechanisms that underlie cilia-associated health and disease.

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Dynein and intraflagellar transport

Abstract: Review article focusing on recent research advancements on the mechanism of intraflagellar transport

Cited by 57 publications

References 86 publications

Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis

Functional exploration of the IFT-A complex in intraflagellar transport and ciliogenesis

Primary Cilia and Mammalian Hedgehog Signaling

Microtubule Motors Drive Hedgehog Signaling in Primary Cilia

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