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Journal ArticleDOI

G protein-coupled receptors stimulation and the control of cell migration.

Mathieu Cotton, +1 more
- 01 Jul 2009 - 
- Vol. 21, Iss: 7, pp 1045-1053
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TLDR
The role of GPCR mediated signal transduction and their importance in the regulation of actin remodeling leading to cell migration are reviewed.
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This article is published in Cellular Signalling.The article was published on 2009-07-01. It has received 238 citations till now. The article focuses on the topics: Actin remodeling & Actin cytoskeleton.

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Citations
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Journal ArticleDOI

Linking actin dynamics and gene transcription to drive cellular motile functions.

TL;DR: The discovery that globular actin polymerization liberates myocardin-related transcription factor (MRTF) cofactors induces the nuclear transcription factor serum response factor (SRF) to modulate the expression of genes encoding structural and regulatory effectors of actin dynamics stimulated research to better understand the actin–MRTF–SRF circuit.
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Endocytic trafficking of Rac is required for the spatial restriction of signaling in cell migration.

TL;DR: It is demonstrated that a Rab5-to-Rac circuitry controls the morphology of motile mammalian tumor cells and primordial germinal cells during zebrafish development, suggesting that this circuitry is relevant for the regulation of migratory programs in various cells, in both in vitro settings and whole organisms.
Journal ArticleDOI

The chemistry, physiology and pathology of pH in cancer

TL;DR: Elevated metabolism, weakened cell-to-capillary diffusive coupling, and adaptations involving H+/H+-equivalent transporters and extracellular-facing CAs give cancer cells the means to manipulate micro-environmental acidity, a cancer hallmark.
Journal ArticleDOI

The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes.

TL;DR: Results indicate that the lipid raft adaptor p18 is essential for anchoring the MEK–ERK pathway to late endosomes, and shed new light on a role of endosomal MEK- ERK pathway in controlling endosome dynamics.
Journal ArticleDOI

Three-dimensional context regulation of metastasis

TL;DR: Synergistic interactions between matrix remodeling and tumor hypoxia influence common mechanisms that maximize tumor progression and cooperate to drive metastasis, which should identify novel therapeutic targets.
References
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PatentDOI

EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF

TL;DR: In this article, agents and methods for growth factor receptor activation by modulating the G-protein mediated signal transduction pathway were described, and a method to activate the growth factor receptors was proposed.
Journal ArticleDOI

Rho GTPases Control Polarity, Protrusion, and Adhesion during Cell Movement

TL;DR: It is concluded that the signal transduction pathways controlled by the four small GTPases, Rho, Rac, Cdc42, and Ras, cooperate to promote cell movement.
Journal ArticleDOI

Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors

TL;DR: It is reported here that the epidermal growth factor receptor (EGFR) and the neu oncoprotein become rapidly tyrosine-phosphorylated upon stimulation of Rat-1 cells with the GPCR agonists endothelin-1, lysophosphatic acid and thrombin, suggesting that there is an intracellular mechanism for transactivation.
Journal ArticleDOI

Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes.

TL;DR: Data suggest that beta-arrestin binding, which terminates receptor-G protein coupling, also initiates a second wave of signal transduction in which the "desensitized" receptor functions as a critical structural component of a mitogenic signaling complex.
Journal ArticleDOI

FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.

TL;DR: Using quantitative assays, it is shown that kinases and adaptor molecules, including focal adhesion kinase, Src, p130CAS, paxillin, extracellular signal-regulated kinase and myosin light-chain kinase are critical for adhesion turnover at the cell front, a process central to migration.
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