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Related Concept Videos

The Ras Gene02:38

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 superfamily...
Small GTPases - Ras and Rho01:24

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:
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
The Ras Gene02:38

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 superfamily...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jul 15, 2026

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
07:49

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

Published on: July 17, 2019

An experimentally derived database of candidate Ras-interacting proteins.

Lawrence E Goldfinger1, Celeste Ptak, Erin D Jeffery

  • 1Division of Rheumatology, Department of Medicine, University of California, San Diego, La Jolla, California 92093, USA. lgoldfinger@ucsd.edu

Journal of Proteome Research
|April 19, 2007
PubMed
Summary

Researchers identified proteins binding to Ras family GTPases using a TAP-tag method. H-Ras interacts with cytoskeletal proteins, while R-Ras and Rap1A bind signaling molecules, creating a database of Ras interactors.

Related Experiment Videos

Last Updated: Jul 15, 2026

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
07:49

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

Published on: July 17, 2019

Area of Science:

  • Molecular biology
  • Cellular signaling
  • Proteomics

Background:

  • Ras GTPases are key regulators of cellular processes.
  • Understanding their interactions is crucial for deciphering cell signaling pathways.
  • Previous interactome studies for these specific Ras proteins in mammalian cells are limited.

Purpose of the Study:

  • To identify novel binding partners for H-Ras, R-Ras, and Rap1A.
  • To establish a comprehensive database of Ras-interacting proteins in mammalian cells.
  • To differentiate interaction profiles among related Ras GTPases.

Main Methods:

  • Utilized a Tandem Affinity Purification (TAP-tag) approach in mouse fibroblasts.
  • Isolated protein complexes associated with H-Ras, R-Ras, and Rap1A.
  • Identified co-purified proteins using nanoflow High-Performance Liquid Chromatography (HPLC) and tandem mass spectrometry.

Main Results:

  • Identified numerous candidate binding proteins for H-Ras, R-Ras, and Rap1A.
  • H-Ras was found to associate with cytoskeletal proteins, including talin-1.
  • R-Ras and Rap1A associated with various membrane-associated signaling molecules.
  • Established the first database of potential Ras interactors in mammalian cells.

Conclusions:

  • The study successfully identified distinct sets of interacting proteins for H-Ras, R-Ras, and Rap1A.
  • The findings provide new insights into the specific cellular functions and pathways regulated by these Ras GTPases.
  • The generated database serves as a valuable resource for future research on Ras signaling.