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  1. Article ; Online: Oscillatory movement of a dynein-microtubule complex crosslinked with DNA origami.

    Abdellatef, Shimaa A / Tadakuma, Hisashi / Yan, Kangmin / Fujiwara, Takashi / Fukumoto, Kodai / Kondo, Yuichi / Takazaki, Hiroko / Boudria, Rofia / Yasunaga, Takuo / Higuchi, Hideo / Hirose, Keiko

    eLife

    2022  Volume 11

    Abstract: Bending of cilia and flagella occurs when axonemal dynein molecules on one side of the axoneme produce force and move toward the microtubule (MT) minus end. These dyneins are then pulled back when the axoneme bends in the other direction, meaning ... ...

    Abstract Bending of cilia and flagella occurs when axonemal dynein molecules on one side of the axoneme produce force and move toward the microtubule (MT) minus end. These dyneins are then pulled back when the axoneme bends in the other direction, meaning oscillatory back and forth movement of dynein during repetitive bending of cilia/flagella. There are various factors that may regulate the dynein activity, e.g. the nexin-dynein regulatory complex, radial spokes, and central apparatus. In order to understand the basic mechanism of dynein's oscillatory movement, we constructed a simple model system composed of MTs, outer-arm dyneins, and crosslinks between the MTs made of DNA origami. Electron microscopy (EM) showed pairs of parallel MTs crossbridged by patches of regularly arranged dynein molecules bound in two different orientations, depending on which of the MTs their tails bind to. The oppositely oriented dyneins are expected to produce opposing forces when the pair of MTs have the same polarity. Optical trapping experiments showed that the dynein-MT-DNA-origami complex actually oscillates back and forth after photolysis of caged ATP. Intriguingly, the complex, when held at one end, showed repetitive bending motions. The results show that a simple system composed of ensembles of oppositely oriented dyneins, MTs, and inter-MT crosslinkers, without any additional regulatory structures, has an intrinsic ability to cause oscillation and repetitive bending motions.
    MeSH term(s) Axonemal Dyneins/metabolism ; Axoneme/metabolism ; Chlamydomonas reinhardtii/metabolism ; DNA/metabolism ; Dyneins/metabolism ; Flagella/physiology ; Microtubules/metabolism ; Movement/physiology
    Chemical Substances DNA (9007-49-2) ; Axonemal Dyneins (EC 3.6.4.2) ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2022-06-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.76357
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Regulatory interplay between Vav1, Syk and β-catenin occurs in lung cancer cells.

    Boudria, Rofia / Laurienté, Vanessa / Oudar, Antonin / Harouna-Rachidi, Souleymane / Dondi, Elisabetta / Le Roy, Christine / Gardano, Laura / Varin-Blank, Nadine / Guittat, Lionel

    Cellular signalling

    2021  Volume 86, Page(s) 110079

    Abstract: Vav1 exhibits two signal transducing properties as an adaptor protein and a regulator of cytoskeleton organization through its Guanine nucleotide Exchange Factor module. Although the expression of Vav1 is restricted to the hematopoietic lineage, its ... ...

    Abstract Vav1 exhibits two signal transducing properties as an adaptor protein and a regulator of cytoskeleton organization through its Guanine nucleotide Exchange Factor module. Although the expression of Vav1 is restricted to the hematopoietic lineage, its ectopic expression has been unraveled in a number of solid tumors. In this study, we show that in lung cancer cells, as such in hematopoietic cells, Vav1 interacts with the Spleen Tyrosine Kinase, Syk. Likewise, Syk interacts with β-catenin and, together with Vav1, regulates the phosphorylation status of β-catenin. Depletion of Vav1, Syk or β-catenin inhibits Rac1 activity and decreases cell migration suggesting the interplay of the three effectors to a common signaling pathway. This model is further supported by the finding that in turn, β-catenin regulates the transcription of Syk gene expression. This study highlights the elaborated connection between Vav1, Syk and β-catenin and the contribution of the trio to cell migration.
    MeSH term(s) Adaptor Proteins, Signal Transducing/metabolism ; Humans ; Lung Neoplasms ; Phosphorylation ; Proto-Oncogene Proteins c-vav/genetics ; Signal Transduction ; Syk Kinase/metabolism ; beta Catenin/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; CTNNB1 protein, human ; Proto-Oncogene Proteins c-vav ; VAV1 protein, human ; beta Catenin ; SYK protein, human (EC 2.7.10.2) ; Syk Kinase (EC 2.7.10.2)
    Language English
    Publishing date 2021-07-09
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1002702-6
    ISSN 1873-3913 ; 0898-6568
    ISSN (online) 1873-3913
    ISSN 0898-6568
    DOI 10.1016/j.cellsig.2021.110079
    Database MEDical Literature Analysis and Retrieval System OnLINE

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