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14 results for “Arp2/3”
Data from: Coordinated ARP2/3 and glycolytic activities regulate the morphological and functional fitness of human CD8+ T cells
<p>CD8<sup>+</sup> T cells rely on actin cytoskeleton remodeling to search for target cells and assemble the immunological synapse (IS) for lethal hit delivery. We here investigated how the energy expenditure related to actin remodeling might influence the fitness of human cytotoxic T cells. We first established that the spreading ability of CD8<sup>+</sup> T cells in conditions of LFA-1 and TCR engagement mirrored the cytotoxic potential of these cells. Morphological and functional fitness were both potentiated by IL-2, which co-stimulated the transcription of glycolytic enzymes, actin isoforms and the subunits of the ARP2/3 complex. This molecular program scaled with F-actin content and cell spreading. Blockade of glycolysis impaired F-actin remodeling at the lamellipodium, chemokine-driven motility and synaptic adhesion, while blockade of mitochondrial OXPHOS affected F-actin less severely and selectively reduced cell elongation during confined migration. Although T cells deficient for the ARP2/3 subunit ARPC1B increased their ATP content upon IL-2 exposure, their morphological and functional defects were only partially corrected, pointing to the pivotal position of ARP2/3 mediated actin polymerization as integrator of T cell energetic state. Our study therefore highlights that the ability of effector T cells to migrate, form IS and ultimately kill target cells depends on a tight coordination of their metabolic and actin remodeling activities.</p>
Distinct roles of the Chlamydia trachomatis effectors TarP and TmeA in the regulation of formin and Arp2/3 during entry
<p>The obligate intracellular pathogen Chlamydia trachomatis manipulates the host actin cytoskeleton to assemble actin-rich structures that drive pathogen entry. The recent discovery of TmeA, which, like TarP, is an invasion-associated type III effector implicated in actin remodeling, raised questions regarding the nature of their functional interaction. Quantitative live-cell imaging of actin remodeling at invasion sites revealed differences in recruitment and turnover kinetics associated with the TarP and TmeA pathways, with the former accounting for most of the robust actin dynamics at invasion sites. TarP-mediated recruitment of actin nucleators, i.e. formins and the Arp2/3 complex, was crucial for rapid actin kinetics, generating a collaborative positive feedback loop that enhanced their respective actin-nucleating activities within invasion sites. In contrast, the formin Fmn1 was not recruited to invasion sites and did not collaborate with Arp2/3 within the context of Tme-aassociated actin recruitment. Although the TarP-Fmn1-Arp2/3 signaling axis is responsible for the majority of actin dynamics, its inhibition had similar effects as the deletion of TmeA on invasion efficiency, consistent with the proposed model that TarP and TmeA act on different stages of the same invasion pathway.</p>
Other Supplementary Material for 'Myosin-I Synergizes with Arp2/3 Complex to Enhance Pushing Forces of Branched Actin Networks' by Xu et al.
<div> <p>Other Supplementary Material for "Myosin-I Synergizes with Arp2/3 Complex to Enhance Pushing Forces of Branched Actin Networks" by Xu, Rutkowski, Rebowski, Boczkowska, Pollard, Dominguez, Vavylonis, and Ostap, bioRxiv, <a href="https://doi.org/10.1101/2024.02.09.579714" rel="nofollow">https://doi.org/10.1101/2024.02.09.579714</a> </p> <p> </p> </div>
Distinct roles of the Chlamydia trachomatis effectors TarP and TmeA in the regulation of formin and Arp2/3 during entry
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Data from: Coordinated ARP2/3 and glycolytic activities regulate the morphological and functional fitness of human CD8+ T cells
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The role of the Arp2/3 complex in shaping the dynamics and structures of branched actomyosin networks
<p>Actomyosin networks give cells the ability to move and divide. These networks contract and expand while being driven by active energy-consuming processes such as motor protein walking and actin polymerization. Actin dynamics is also regulated by actin-binding proteins, such as the actin-related protein 2/3 (Arp2/3) complex. This complex generates branched filaments thereby changing the overall organization of the network. In this work, the spatiotemporal patterns of dynamical actin assembly accompanying the branching-induced reorganization caused by Arp2/3 were studied using a computational model (MEDYAN); this model simulates actomyosin network dynamics as a result of chemical reactions whose rates are modulated by rapid mechanical equilibration. We show that branched actomyosin networks relax significantly more slowly than do unbranched networks. Also, branched networks undergo rare convulsive movements, “avalanches”, that release strain in the network. These avalanches are associated with the more heterogeneous distribution of mechanically-linked filaments displayed by branched networks. These far-from equilibrium events arising from the marginal stability of growing actomyosin networks provide a possible mechanism of the “cytoquakes” recently seen in experiments.</p>
Partial de-repression of the hyphal program does not restore hyphae formation in absence of a functional Arp2/3 complex
GEO Series GSE19582. Candida albicans. 6 samples. Type: Expression profiling by array.
Knockout of the Arp2/3 complex in epidermis causes a psoriasis-like disease hallmarked by hyperactivation of transcription factor Nrf2
GEO Series GSE107266. Mus musculus. 9 samples. Type: Expression profiling by high throughput sequencing.
Knockout of the Arp2/3 complex in epidermis causes a psoriasis-like disease hallmarked by hyperactivation of transcription factor Nrf2 [Keratinocytes ssRNA-Seq]
GEO Series GSE107264. Mus musculus. 3 samples. Type: Expression profiling by high throughput sequencing.
Arp2/3 Complex Activity Enables Nuclear YAP for Naïve Pluripotency of Human Embryonic Stem Cells
GEO Series GSE276968. Homo sapiens. 12 samples. Type: Expression profiling by high throughput sequencing.
Arp2/3 complex activity is necessary for mouse ESC differentiation, times formative pluripotency, and enables lineage specification
GEO Series GSE175391. Mus musculus. 9 samples. Type: Expression profiling by high throughput sequencing.
Forward genetics in Candida albicans reveals the Arp2/3 complex is required for hyphal formation, but not endocytosis
GEO Series GSE19583. Candida albicans. 18 samples. Type: Expression profiling by array.
Knockout of the Arp2/3 complex in epidermis causes a psoriasis-like disease hallmarked by hyperactivation of transcription factor Nrf2 [Epidermis ssRNA-Seq]
GEO Series GSE107265. Mus musculus. 6 samples. Type: Expression profiling by high throughput sequencing.
Arp2/3 complex mutants show a pronounced lack of hyphal specific gene expression in Candida albicans
GEO Series GSE19565. Candida albicans. 12 samples. Type: Expression profiling by array.
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