Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain

Ichikawa, Muneyoshi; Saito, Kei; Yanagisawa, Haruaki; Yagi, Toshiki; Kamiya, Ritsu; Yamaguchi, Satoshi; Yajima, Junichiro; Kushida, Yasuharu; Nakano, Kentaro; Numata, Osamu; Toyoshima, Yoko Y.

doi:10.1091/mbc.e15-05-0289

Cited by 27 publications

(33 citation statements)

References 49 publications

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“…One involving the central pair and radial spokes that impacts the inner arms, and second distinct system that activates the outer arms. This second system is thought to involve the highly conserved leucine-rich repeat protein LC1 (Benash- ski et al 1999;Wu et al 2000) that has recently been shown to bind the microtubule-binding domain of the g heavy chain (Ichikawa et al 2015). When mutant forms of this protein are expressed in a wild-type background, they yield dominant negative effects that have dramatic consequences on swimming velocity and on the ability of the cilia to maintain hydrodynamic coupling (Patel- King and King 2009;Rompolas et al 2010).…”

Section: Dynein Motor Function and Regulationmentioning

confidence: 99%

Axonemal Dynein Arms

King

2016

Cold Spring Harb Perspect Biol

126

125

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Axonemal dyneins form the inner and outer rows of arms associated with the doublet microtubules of motile cilia. These enzymes convert the chemical energy released from adenosine triphosphate (ATP) hydrolysis into mechanical work by causing the doublets to slide with respect to each other. Dyneins form two major groups based on the number of heavy-chain motors within each complex. In addition, these enzymes contain other components that are required for assembly of the complete particles and/or for the regulation of motor function in response to phosphorylations status, ligands such as Ca, changes in cellular redox state and which also apparently monitor and respond to the mechanical state or curvature in which any given motor finds itself. It is this latter property, which is thought to result in waves of motor function propagating along the axoneme length. Here, I briefly describe our current understanding of axonemal dynein structure, assembly, and organization.

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Section: Dynein Motor Function and Regulationmentioning

confidence: 99%

Axonemal Dynein Arms

King

2016

Cold Spring Harb Perspect Biol

126

125

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“…Chemically modified gold nanoparticles visualize the tagged sites within protein complexes (Ichikawa et al, 2015;Guesdon et al, 2016;Song et al, 2014). Using gold nanoparticles with diameter less than 5 nm (Kitai et al 2011), the specific sites within ~30 nm CC1-protrusion (Figure 3, Figure 3-S1) and ~20 nm CC2-neck (Figure 4) were clearly discernible.…”

Section: Labeling Of Flexible Objects By Gold Nanoparticlesmentioning

confidence: 99%

Domain organization and conformational change of dynactin p150

Saito

Murayama

Hata

et al. 2018

Preprint

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Dynactin is a principal regulator of the minus-end directed microtubule motor dynein. The sidearm of dynactin is essential for binding to microtubules and regulation of dynein activity. Although our understanding of the structure of the dynactin backbone (Arp1 rod) has greatly improved recently, structural details of the sidearm part remain elusive. Here, electron microscopy of individual molecules of the dynactin complex revealed that the sidearm was highly flexible and exhibited diverse morphologies.Utilizing mutants for nanogold labeling and deletion analysis, we determined the domain organization of the largest subunit p150 and identified a filamentous structure protruding from the head domain of the sidearm as the coiled-coil 1 (CC1), the dynein-binding domain, in p150. Furthermore, the protrusion formed by CC1 exhibited either a folded or an extended form, suggesting that CC1 works as an extending "arm". These findings provide clues to understand how dynactin binds to microtubules and regulates dynein.

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“…Furthermore, it has been widely assumed that LC1 associates with AAA1 and AAA3 or AAA4 of the AAA+ ring in the gamma heavy chain of OAD (OADγ) in C. reinhardtii (Benashski et al 1999). However, it was recently reported that LC1 is tightly bound to the MTBD of OADγ, which is located at the tip of stalk region in the motor domain (Ichikawa et al 2015). This was the first report of an LC interacting with the MTBD.…”

Section: Light Chainmentioning

confidence: 92%

“…This was the first report of an LC interacting with the MTBD. Moreover, it was also discovered that the binding of LC1 to the MTBD decreases the MT-binding affinity of the HC (Ichikawa et al 2015). Because it has been reported that the ATPase activity of the HC is increased in the presence of MTs (Kon et al 2009), both results imply that LC1 indirectly changes the ATPase activity of OADγ and regulates ciliary/ flagellar beating.…”

Section: Light Chainmentioning

confidence: 95%

Structural atlas of dynein motors at atomic resolution

2018

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Dynein motors are biologically important bio-nanomachines, and many atomic resolution structures of cytoplasmic dynein components from different organisms have been analyzed by X-ray crystallography, cryo-EM, and NMR spectroscopy. This review provides a historical perspective of structural studies of cytoplasmic and axonemal dynein including accessory proteins. We describe representative structural studies of every component of dynein and summarize them as a structural atlas that classifies the cytoplasmic and axonemal dyneins. Based on our review of all dynein structures in the Protein Data Bank, we raise two important points for understanding the two types of dynein motor and discuss the potential prospects of future structural studies.

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Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain

Cited by 27 publications

References 49 publications

Axonemal Dynein Arms

Axonemal Dynein Arms

Domain organization and conformational change of dynactin p150

Structural atlas of dynein motors at atomic resolution

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