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The Ras Gene

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The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
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MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Related Experiment Video

Updated: May 5, 2026

RhoC GTPase Activation Assay

RhoC GTPase Activation Assay

Published on: August 23, 2010

Integrin activation by R-ras

Z Zhang¹, K Vuori, H Wang

¹La Jolla Cancer Research Center, The Burnham Institute, California 92037, USA.

|April 5, 1996

Summary

This summary is machine-generated.

Activated R-ras signaling transforms suspension cells into adherent ones by enhancing integrin binding affinity and fibronectin matrix assembly. This study reveals R-ras

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Area of Science:

Cell biology
Molecular biology
Biochemistry

Background:

Integrins are crucial cell surface receptors mediating cell adhesion.
R-ras is a small GTPase implicated in cell signaling pathways.
Regulation of integrin activity is vital for cellular processes.

Purpose of the Study:

To investigate the role of R-ras in regulating integrin-mediated cell adhesion.
To elucidate the mechanism by which R-ras influences integrin function.

Main Methods:

Transfection of cell lines with constitutively active and dominant-negative R-ras mutants.
Assessment of cell adhesion to integrin ligands.
Measurement of integrin-ligand binding affinity.
Quantification of fibronectin matrix assembly.

Main Results:

Constitutively active R-ras expression induced high cell adhesion in suspension cells.
Activated R-ras enhanced integrin binding affinity and fibronectin matrix formation.
Dominant-negative R-ras reduced endogenous R-ras-mediated cell adhesiveness.

Conclusions:

R-ras plays a key role in modulating integrin ligand-binding activity.
Activated R-ras promotes cell adhesion through enhanced integrin function.
Endogenous R-ras regulates endogenous integrin adhesiveness, suggesting a novel regulatory mechanism.