Dynein and intraflagellar transport

Witman, George B.; Hou, Yuqing

doi:10.1016/b978-0-12-809471-6.00013-9

Cited by 3 publications

(5 citation statements)

References 137 publications

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“…Based on studies in a range of organisms, dynein-2 is now recognized as the ubiquitous motor for retrograde IFT in motile and sensory cilia ( Box 1 ) [ 22 ]. The IFT system moves axonemal building blocks, regulatory proteins, and signaling molecules within the cilium [ 23 – 26 ] and powers surface gliding locomotion of protozoa [ 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

“…The premise of this review is to compare dynein-1 and -2 in terms of their operating environment, subunit composition, motility, and regulation, asking: which molecular adaptations may engender their physiological roles? For comprehensive reviews of each dynein individually, the reader is referred to recent articles [ 7 – 11 , 22 ].…”

Section: Introductionmentioning

confidence: 99%

“…There is compelling evidence that, in contrast with the dynein-1 intermediate chain, WDR34 does not homodimerize: the endogenous protein fails to co-immunoprecipitate with GFP (green fluorescent protein)-tagged WDR34 expressed in RPE1 cells [ 72 ]. Rather, biochemical studies point to a model in which WDR34 exists in a sub-complex with WDR60 and light chains, which in turn forms a metastable interaction with the dynein-2 heavy chain and light-intermediate chain [ 22 , 72 , 75 , 80 ].…”

Section: Introductionmentioning

confidence: 99%

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Emerging mechanisms of dynein transport in the cytoplasm versus the cilium

Roberts

2018

Biochemical Society Transactions

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Two classes of dynein power long-distance cargo transport in different cellular contexts. Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior. Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella. Both dyneins operate as large ATP-driven motor complexes, whose dysfunction is associated with a group of human disorders. But how similar are their mechanisms of action and regulation? To examine this question, this review focuses on recent advances in dynein-1 and -2 research, and probes to what extent the emerging principles of dynein-1 transport could apply to or differ from those of the less well-understood dynein-2 mechanoenzyme.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Emerging mechanisms of dynein transport in the cytoplasm versus the cilium

Roberts

2018

Biochemical Society Transactions

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“…Cytoplasmic dynein-2 is responsible for intraflagellar transport along MTs in cilia and flagella. 11 Cytoplasmic dynein-1 (henceforth termed dynein) is ubiquitous across cell types and is the primary motor responsible for the transport of cargo toward the minus ends of MTs in the cytoplasm. 12 Specifically, dynein is required for the orientation of the bipolar spindle, 13 kinetochore separation during cell division, 14 and long-range, minus end-directed intracellular transport during interphase.…”

mentioning

confidence: 99%

“…The cytoplasmic dynein family consists of two motors, namely, cytoplasmic dynein-1 and -2. Cytoplasmic dynein-2 is responsible for intraflagellar transport along MTs in cilia and flagella . Cytoplasmic dynein-1 (henceforth termed dynein) is ubiquitous across cell types and is the primary motor responsible for the transport of cargo toward the minus ends of MTs in the cytoplasm …”

mentioning

confidence: 99%

Role of Dynactin in the Intracellular Localization and Activation of Cytoplasmic Dynein

Tirumala

Parton

2019

Biochemistry

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Cytoplasmic dynein, the major minus end-directed motor protein in several cell types, transports a variety of intracellular cargo upon forming a processive tripartite complex with its activator dynactin and cargo adaptors such as Hook3 and BicD2. Our current understanding of dynein regulation stems from a combination of in vivo studies of cargo movement upon perturbation of dynein activity, in vitro single-molecule experiments, and cryo-electron microscopy studies of dynein structure and its interaction with dynactin and cargo adaptors. In this Perspective, we first consolidate data from recent publications to understand how perturbations to the dynein–dynactin interaction and dynactin’s in vivo localization alter the behavior of dynein-driven cargo transport in a cell type- and experimental condition-specific manner. In addition, we touch upon results from in vivo and in vitro studies to elucidate how dynein’s interaction with dynactin and cargo adaptors activates dynein and enhances its processivity. Finally, we propose questions that need to be addressed in the future with appropriate experimental designs so as to improve our understanding of the spatiotemporal regulation of dynein’s function in the context of the distribution and dynamics of dynactin in living cells.

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Cytoplasmic factories for axonemal dynein assembly

King

2021

Journal of Cell Science

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Axonemal dyneins power the beating of motile cilia and flagella. These massive multimeric motor complexes are assembled in the cytoplasm, and subsequently trafficked to cilia and incorporated into the axonemal superstructure. Numerous cytoplasmic factors are required for the dynein assembly process, and, in mammals, defects lead to primary ciliary dyskinesia, which results in infertility, bronchial problems and failure to set up the left-right body axis correctly. Liquid–liquid phase separation (LLPS) has been proposed to underlie the formation of numerous membrane-less intracellular assemblies or condensates. In multiciliated cells, cytoplasmic assembly of axonemal dyneins also occurs in condensates that exhibit liquid-like properties, including fusion, fission and rapid exchange of components both within condensates and with bulk cytoplasm. However, a recent extensive meta-analysis suggests that the general methods used to define LLPS systems in vivo may not readily distinguish LLPS from other mechanisms. Here, I consider the time and length scales of axonemal dynein heavy chain synthesis, and the possibility that during translation of dynein heavy chain mRNAs, polysomes are crosslinked via partially assembled proteins. I propose that axonemal dynein factory formation in the cytoplasm may be a direct consequence of the sheer scale and complexity of the assembly process itself.

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Dynein and intraflagellar transport

Cited by 3 publications

References 137 publications

Emerging mechanisms of dynein transport in the cytoplasm versus the cilium

Emerging mechanisms of dynein transport in the cytoplasm versus the cilium

Role of Dynactin in the Intracellular Localization and Activation of Cytoplasmic Dynein

Cytoplasmic factories for axonemal dynein assembly

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