Results 71 to 80 of about 316,202 (350)
Actin cytoskeleton in dendritic spine
Folia Pharmacologica Japonica, 2007 樹状突起スパインは脳内の主要な興奮性シナプス後部であり，その形態および構成タンパク質の可塑的変化は学習記憶などの高次機能に重要である．スパイン内の構造体としては，シナプス後部肥厚（PSD）とアクチン細胞骨格があり，スパインの形態変化は主にアクチン細胞骨格により制御されている．スパイン内ではその頭部と頸部でアクチン線維の構造が異なることに加えて，頭部の中でもシナプス直下のPSD近傍と細胞質の中心領域でアクチン結合タンパク質の分布が異なる．したがって，スパインは3種類の性質の異なるアクチン細胞骨格によって構成されていると考えられる．アクチンを脱重合させると，多くのスパイン構成タンパク質の局在が不安定化し，スパイン形態もフィロポディア様に変化する．従って，アクチン細胞骨格がスパイン形態の形成 ...
Kenji, Hanamura, Tomoaki, Shirao
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Bacterial toxins modifying the actin cytoskeleton [PDF]
, 2010 Numerous bacterial toxins recognize the actin cytoskeleton as a target. The clostridial binary toxins (Iota and C2 families) ADP-ribosylate the actin monomers causing the dissociation of the actin filaments.
Claude Bouchaud +5 more
core +2 more sources
Patterns in Space: Coordinating Adhesion and Actomyosin Contractility at E-cadherin Junctions
, 2013 Cadherin adhesion receptors are fundamental determinants of tissue organization in health and disease. Increasingly, we have come to appreciate that classical cadherins exert their biological actions through active cooperation with the contractile actin ...
Wu, Selwin K., Yap, Alpha S.
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Molecular Oncology, EarlyView.HDAC4 is degraded by the E3 ligase FBXW7. In colorectal cancer, FBXW7 mutations prevent HDAC4 degradation, leading to oxaliplatin resistance. Forced degradation of HDAC4 using a PROTAC compound restores drug sensitivity by resetting the super‐enhancer landscape, reprogramming the epigenetic state of FBXW7‐mutated cells to resemble oxaliplatin ...
Vanessa Tolotto +13 more
wiley +1 more source
Effects of F/G-actin ratio and actin turn-over rate on NADPH oxidase activity in microglia
BMC Immunology, 2010 Background Most in vivo studies that have addressed the role of actin dynamics in NADPH oxidase function in phagocytes have used toxins to modulate the polymerization state of actin and mostly effects on actin has been evaluated by end point measurements
Rasmussen Izabela +5 more
doaj +1 more source
Dual targeting of RET and SRC synergizes in RET fusion‐positive cancer cells
Molecular Oncology, EarlyView.Despite the strong activity of selective RET tyrosine kinase inhibitors (TKIs), resistance of RET fusion‐positive (RET+) lung cancer and thyroid cancer frequently occurs and is mainly driven by RET‐independent bypass mechanisms. Son et al. show that SRC TKIs significantly inhibit PAK and AKT survival signaling and enhance the efficacy of RET TKIs in ...
Juhyeon Son +13 more
wiley +1 more source
Interactions between plant endomembrane systems and the actin cytoskeleton
Frontiers in Plant Science, 2015 Membrane trafficking, organelle movement and morphogenesis in plant cells are mainly controlled by the cytoskeleton. Not all proteins that regulate the actin cytoskeleton and membrane dynamics in animal systems have functional homologues in plants ...
Pengwei eWang, Patrick J. Hussey
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A novel function of twins, B subunit of protein phosphatase 2A, in regulating actin polymerization. [PDF]
PLoS ONE, 2017 Actin is an important component of the cytoskeleton and its polymerization is delicately regulated by several kinases and phosphatases. Heterotrimeric protein phosphatase 2A (PP2A) is a potent phosphatase that is crucial for cell proliferation, apoptosis,
Po-An Yeh, Ching-Jin Chang
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Oxidation and reduction of actin: Origin, impact in vitro and functional consequences in vivo
European Journal of Cell Biology, 2022 Actin is among the most abundant proteins in eukaryotic cells and assembles into dynamic filamentous networks regulated by many actin binding proteins. The actin cytoskeleton must be finely tuned, both in space and time, to fulfill key cellular functions
Clémentine Rouyère +3 more
doaj +1 more source
Ultrastructure of the actin cytoskeleton [PDF]
Current Opinion in Cell Biology, 2018 The actin cytoskeleton is the primary force-generating machinery in the cell, which can produce pushing (protrusive) forces using energy of actin polymerization and pulling (contractile) forces via sliding of bipolar filaments of myosin II along actin filaments, as well as perform other key functions.
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