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The Ras Gene

The Ras Gene

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.
Ras is a...

Small GTPases - Ras and Rho

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:

Rab Cascades

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.

GTPases and their Regulation

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒ small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...

GTPases and their Regulation

GTPases and their Regulation

Rab Proteins

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

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Related Experiment Video

Updated: Apr 18, 2026

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

Published on: July 17, 2019

Cooperation between Noncanonical Ras Network Mutations.

Edward C Stites¹, Paul C Trampont², Lisa B Haney³

¹Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA; Clinical Translational Research Division, Translational Genomics Research Institute, Phoenix, AZ 85004, USA.

|January 21, 2015

Summary

Cancer mutations often work together. Mutations in the tumor suppressor gene NF1 can amplify Ras pathway mutations, driving cancer development. This suggests combinations of mutations, not just single ones, can be cancer drivers.

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Last Updated: Apr 18, 2026

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

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Published on: July 17, 2019

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

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Published on: October 8, 2015

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Area of Science:

Oncology
Computational Biology
Genetics

Background:

Cancer arises from accumulated mutations leading to a specific phenotype.
The cooperative mechanisms and selection pressures for mutation combinations remain unclear.

Purpose of the Study:

To investigate how combinations of mutations within the Ras signaling network contribute to cancer development.
To explore the role of the NF1 tumor suppressor gene in modulating the effects of Ras pathway mutations.

Main Methods:

Development of a mathematical model for the Ras signaling network.
Inclusion of computational random mutagenesis simulations.
Analysis of large-scale cancer genomic datasets.

Main Results:

NF1 mutations were found to amplify the effects of other Ras pathway mutations, including noncanonical Ras mutants.
Increased co-occurrence of NF1 mutations with other Ras network gene mutations was observed in cancer genomic data.
These findings suggest that combinations of Ras pathway mutations act as cancer drivers.

Conclusions:

Combinations of Ras pathway mutations, particularly those involving NF1, can drive cancer phenotypes.
Network instability resulting from mutation combinations may promote cancer, similar to genomic instability.