Ras and Rho GTPases: a family reunion

Article Abstract:

Physiological aspects of cross-communication between Ras and Rho family of GTPases in animal cells is discussed. Results demonstrate that gene expression, cell proliferation, transformation, and migration are controlled by combinatorial activities in a synergistic manner. Data further indicate that distinct GTPases are activated in response to specific agonists.

United Kingdom, Research, Cellular signal transduction, Physiological regulation, Biological control systems, Cell interaction, Cell interactions

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Structural evidence for feedback activation by Ras-GTP of the Ras-specific nucleotide exchange factor SOS

Article Abstract:

The Ras protein binds to the catalytic module of SOS at a conservative site, specific for Ras-GTP, and is situated distal to the active site. Crystallographic analyses indicate that Ras-GTP stabilizes SOS active site and forms ternary complexes with SOS(sup)cat, enhancing nucleotide release from Ras.

Proteins, Structure-activity relationships (Biochemistry), Structure

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Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

Article Abstract:

The cdc42, a member of rho family in Swiss 3T3 cells, activates rho and rac for cell motility. Rac and rho are the members of ras-related GTPases. Rho polymerizes actin to form stress fibers and controls the formation of focal adhesion complexes. The rac produces lamellipodia from the actin structure. The cdc42 forms filopodia of the actin structure at the cell periphery and also regulates the assembly of focal adhesion complexes at the plasma membrane. Lamellipodia and filopodia complexes contain vinculin, paxillin and focal adhesion kinase.

Cells, Actin, Cell migration

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