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Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65(super PAK) and the JNK/SAPK MAP kinase cascade

Article Abstract:

Rac and Cdc42 belong to the Rho family of GTP-binding proteins involved in the formation of polymerized actin structures and the assembly of associated integrin complexes. They also stimulate kinase cascades leading to the activation of JNK/SAPK and wild-type p65(super PAK). Herein, a Y40C substitution in Rac and Cdc42 abolished their ability to activate p65(super PAK) or the JNK/SAPK MAP kinase cascade but did not inhibit their ability to induce lamellipodia and fillipodia. However, Rac failed to induce the formation of lamellipodia when a F37A effector site substitution was introduced. These results suggest that the mechanism of action of Rac and Cdc42 is mediated by distinct, independent downstream signals.

Author: Hall, Alan, Stowers, Lisa, Chant, John, Aspenstrom, Pontus, Lamarche, Nathalie, Tapon, Nicholas, Burbelo, Peter D., Bridges, Tina
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Cell cycle

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GTPase cascades choreographing cellular behavior: movement, morphogenesis, and more

Article Abstract:

The Ras-related GTPase controls the cytoskeleton. GTPase cascades regulate movement, morphogenesis and potential for choreographing cellular behavior. A GTPase cascade has one GTPase regulate the action of another GTPase. GTP-bound form and GDP-bound form are the two conformations of GTPase. The GTP-bound form is active and sends a signal but the GDP form is inactive and sends no signal. Functions like vesicular transport, translation, growth control, apoptosis and nuclear import are controlled by GTPases.

Author: Stowers, Lisa, Chant, John
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
Analysis, Observations, Cytoskeleton

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Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta

Article Abstract:

Results show that protein kinasezeta activity, expressed via the microtubule motor protein dynein, mediates cell polarity in eukaryotic cells. Data indicate that the localized activation of integrins at the cell front initiates a signal transduction process, which leads to Cdc42 activation, also involved in cell polarity pathway.

Author: Hall, Alan, Etienne-Manneville, Sandrine
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
United Kingdom, Physiological aspects, Cellular signal transduction, Polarity (Biology), Astrocytes, Integrins

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Subjects list: Research, G proteins
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