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Journal ArticleDOI

Proteins regulating Ras and its relatives.

Mark S. Boguski, +1 more
- 16 Dec 1993 - 
- Vol. 366, Iss: 6456, pp 643-654
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TLDR
Many of these proteins are much larger and more complex than their targets, containing multiple domains capable of interacting with an intricate network of cellular enzymes and structures.
Abstract
GTPases of the Ras superfamily regulate many aspects of cell growth, differentiation and action. Their functions depend on their ability to alternate between inactive and active forms, and on their cellular localization. Numerous proteins affecting the GTPase activity, nucleotide exchange rates and membrane localization of Ras superfamily members have now been identified. Many of these proteins are much larger and more complex than their targets, containing multiple domains capable of interacting with an intricate network of cellular enzymes and structures.

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Citations
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Journal ArticleDOI

Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

TL;DR: It is reported here that cdc42, another member of the rho family, triggers the formation of a third type of actin-based structure found at the cell periphery, filopodia, in addition to stress fibers, and rho controls the assembly of focal adhesion complexes.
Journal ArticleDOI

SMART, a simple modular architecture research tool: Identification of signaling domains

TL;DR: SMART as discussed by the authors is a web-based tool that allows rapid identification and annotation of signaling domain sequences, which can be used to determine the modular architectures of single sequences or genomes.

SMART, a simple modular architecture research tool: Identification of signaling domains (computer analysisydiacylglycerol kinasesyDEATH domainydisease genesyautomatic sequence annotation)

TL;DR: SMART as discussed by the authors is a web-based tool that allows rapid identification and annotation of signaling domain sequences, which can be used to determine the modular architectures of single sequences or genomes.
Journal ArticleDOI

Small GTP-Binding Proteins

TL;DR: In this review, functions of small G proteins and their modes of activation and action are described.
Journal ArticleDOI

Protein modules and signalling networks

TL;DR: This work highlights conserved protein domains that act as key regulatory participants in many of these different signalling pathways in multicellular organisms.
References
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Journal ArticleDOI

The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors.

Anne J. Ridley, +1 more
- 07 Aug 1992 - 
TL;DR: Rho, a ras-related GTP-binding protein, rapidly stimulated stress fiber and focal adhesion formation when microinjected into serum-starved Swiss 3T3 cells, implying that rho is essential specifically for the coordinated assembly of focal adhesions and stress fibers induced by growth factors.
Journal ArticleDOI

The small GTP-binding protein rac regulates growth factor-induced membrane ruffling.

TL;DR: It is proposed that rac and rho are essential components of signal transduction pathways linking growth factors to the organization of polymerized actin and that growth factors act through rac to stimulate this rho-dependent response.
Journal ArticleDOI

The GTPase superfamily: conserved structure and molecular mechanism

TL;DR: GTPases are conserved molecular switches, built according to a common structural design, and rapidly accruing knowledge of individual GTPases—crystal structures, biochemical properties, or results of molecular genetic experiments—support and generate hypotheses relating structure to function in other members of the diverse family of GTPase.
Journal ArticleDOI

The GTPase superfamily: a conserved switch for diverse cell functions

TL;DR: A molecular switch is a molecular switch whose "on" and "off" states are triggered by binding and hydrolysis of GTP as discussed by the authors. But the mechanism in myriad versions of the switch can be traced back to a single primordial protein.
Journal ArticleDOI

Mammalian Ras interacts directly with the serine/threonine kinase Raf

TL;DR: Raf interacts with wild-type and activated Ras, but not with an effector domain mutant of Ras or with a dominant-interfering Ras mutant, and this interaction is dependent on GTP bound to Ras.
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