Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport

Barbosa, Daniel José; Duro, Joana; Prevo, Bram; Cheerambathur, Dhanya K.; Carvalho, Alexandra T. P.; Gassmann, Reto

doi:10.1371/journal.pgen.1006941

Cited by 38 publications

(46 citation statements)

References 77 publications

(88 reference statements)

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“…Therefore, it is consistent with the findings that active functions of these cellular processes through ECM were the main cause for tumor development, progression and metastasis. Tubulin binding, microtubule binding and microtubule motor activity were associated with decreased muscle function-mediated cytoskeleton remodeling in cancer development and progression [26,27,28].…”

Section: Plos Onementioning

confidence: 99%

DNA methylation biomarkers for nasopharyngeal carcinoma

et al. 2020

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Background Aberrant methylation of DNA plays an important role in the pathogenesis of nasopharyngeal carcinoma (NPC). In the current study, we aimed to integrate three cohorts profile datasets to identify abnormally methylated-differentially expressed genes and pathways associated with NPC. Methods Data of gene expression microarrays (GSE53819, GSE412452) and gene methylation microarrays (GSE52068) obtained from the GEO database. Aberrantly methylated differentially expressed genes (DEGs) were obtained by GEO2R. The David database was utilized to perform enrichment and functional analysis regarding selected genes. To create a protein-protein interaction (PPI), STRING and Cytoscape software were utilized. The MCODE was used for module analysis of the PPI network. Results In total, 181 hypomethylation-high expression genes were identified, which were enriched in the biological mechanisms involved in the differentiation of endodermal cell, mitotic nuclear division, mitotic cell cycle process, chromosome segregation and cell cycle phase transition, etc. Pathway enrichment showed ECM-receptor interaction, PI3K-Akt signaling pathway, Focal adhesion, Protein digestion and absorption and Amoebiasis, etc. The top 3 hub genes of PPI network were FANCI, POSTN, and IFIH1. Additionally, 210 hypermethylation-low expression genes were identified, and our data revealed enrichment in biological processes including axoneme assembly, micro tubular formation, assembly of axonemal dynein

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Section: Plos Onementioning

confidence: 99%

DNA methylation biomarkers for nasopharyngeal carcinoma

et al. 2020

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“…The cortical-localized NuMA forms the cortical force generating machinery (Kiyomitsu and Cheeseman, 2012;Kiyomitsu and Cheeseman, 2013;Okumura et al, 2018;Kiyomitsu, 2019). The recruitment of dynein to the plus end of the microtubules depends on dynactin and EBs, and contributes to the initiation of transport (Moughamian and Holzbaur, 2012;Barbosa et al, 2017;Jha et al, 2017). HOOK proteins recruit dynein to the early endosomes and nuclear envelope (Bielska et al, 2014;Zhang et al, 2014;Guo et al, 2016;Dwivedi et al, 2019).…”

Section: Layer 3: Regulation Of the Dynein Complex Through Accessory mentioning

confidence: 99%

“…Whereas dynein contributes to the focusing of microtubules at spindle poles (Verde et al, 1991;Heald et al, 1996Heald et al, , 1997Merdes et al, 2000;Goshima et al, 2005;Morales-Mulia and Scholey, 2005;Raaijmakers et al, 2013;Dwivedi et al, 2019), an in vitro reconstituted study demonstrated that dynein-dynactin-BICD2 complexes can organize the aster MT array through clustering at the minus end of microtubules (Tan et al, 2018). The accumulation of dynein-dynactin-BICD2 complex is regulated by the tyrosination of the C-terminus of α-tubulin, which affects the affinity of dynactin complex to microtubules (McKenney et al, 2016;Barbosa et al, 2017).…”

Section: Network Of Dyneinsmentioning

confidence: 99%

The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division

Torisawa

Kimura

2020

Front. Cell Dev. Biol.

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Cytoplasmic dynein-1 (hereafter referred to as dynein) is a major microtubule-based motor critical for cell division. Dynein is essential for the formation and positioning of the mitotic spindle as well as the transport of various cargos in the cell. A striking feature of dynein is that, despite having a wide variety of functions, the catalytic subunit is coded in a single gene. To perform various cellular activities, there seem to be different types of dynein that share a common catalytic subunit. In this review, we will refer to the different kinds of dynein as "dyneins." This review attempts to classify the mechanisms underlying the emergence of multiple dyneins into four layers. Inside a cell, multiple dyneins generated through the multi-layered regulations interact with each other to form a network of dyneins. These dynein networks may be responsible for the accurate regulation of cellular activities, including cell division. How these networks function inside a cell, with a focus on the early embryogenesis of Caenorhabditis elegans embryos, is discussed, as well as future directions for the integration of our understanding of molecular layering to understand the totality of dynein's function in living cells.

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“…L4 hermaphrodites injected with dsRNA were grown for 40 h on NGM plates containing OP50 bacteria, single adults were placed on new mating plates (NGM plates with a small amount of OP50 bacteria) and removed 8 h later. The number of hatched and unhatched embryos on each plate was counted after further incubation for 16 h. Immunofluorescence in C. elegans embryos was carried out as described [47], using the following primary antibodies: goat anti-GFP, 1:15000; rabbit anti-mCherry OD78, 1 µg/mL; mouse anti-a-Tubulin DM1a, 1:1000 (Sigma-Aldrich); mouse anti-FLAG M2, 1:1000 (Sigma-Aldrich); rabbit anti-KNL-1 OD33, 1 µg/mL; rabbit anti-BUB-1 OD31, 1 µg/mL; rabbit anti-ZWL-1 OD85, 1 µg/mL; rabbit anti-SPDL-1 OD164, 1:7000. Antibodies OD31, OD33, OD78, OD85, and OD164 were a gift from Arshad Desai.…”

Section: Embryonic Viabilitymentioning

confidence: 99%

Self-assembly of the RZZ complex into filaments drives kinetochore expansion in the absence of microtubule attachment

Gassmann

Pereira

Reis

et al. 2018

Preprint

Self Cite

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SUMMARYThe kinetochore is a dynamic multi-protein assembly that forms on each sister chromatid and interacts with microtubules of the mitotic spindle to drive chromosome segregation. In animals, kinetochores without attached microtubules expand their outermost layer into crescent and ring shapes to promote microtubule capture and spindle assembly checkpoint (SAC) signalling. Kinetochore expansion is an example of protein co-polymerization, but the mechanism is not understood. Here, we present evidence that kinetochore expansion is driven by oligomerization of the Rod-Zw10-Zwilch (RZZ) complex, an outer kinetochore component that recruits the motor dynein and the SAC proteins Mad1-Mad2. Depletion of ROD in human cells suppresses kinetochore expansion, as does depletion of Spindly, the adaptor that connects RZZ to dynein, while dynein itself is dispensable. Expansion is also suppressed by mutating ZWILCH residues implicated in Spindly binding. Conversely, supplying cells with excess ROD facilitates kinetochore expansion under otherwise prohibitive conditions. Using the C. elegans early embryo, we demonstrate that ROD-1 has a concentration-dependent propensity for oligomerizing into µm-scale filaments, and we identify the ROD-1 β-propeller as a key regulator of self-assembly. Finally, we show that a minimal ROD-1-Zw10 complex efficiently oligomerizes into filaments in vitro. Our results suggest that RZZ’s capacity for oligomerization is harnessed by kinetochores to assemble the expanded outermost domain, in which RZZ filaments serve as recruitment platforms for SAC components and microtubule-binding proteins. Thus, we propose that RZZ self-assembly into filaments underlies the adaptive change in kinetochore size that contributes to chromosome segregation fidelity.

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Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport

Cited by 38 publications

References 77 publications

DNA methylation biomarkers for nasopharyngeal carcinoma

DNA methylation biomarkers for nasopharyngeal carcinoma

The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division

Self-assembly of the RZZ complex into filaments drives kinetochore expansion in the absence of microtubule attachment

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