Related Experiment Video

Updated: May 13, 2026

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay

Published on: November 11, 2018

Nonredundant functions for Ras GTPase-activating proteins in tissue homeostasis

Philip D King1, Beth A Lubeck, Philip E Lapinski

  • 1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. kingp@umich.edu

Science Signaling
|February 28, 2013
PubMed

Insights

Ras guanosine triphosphatase-activating proteins (RasGAPs) inactivate Ras proteins during cell signaling. Genetic studies reveal unique roles for each RasGAP in maintaining tissue health and preventing disease.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Genetics

Background:

  • Ras proteins are key regulators of cell signaling, and their inactivation is crucial for proper cellular function.
  • Ras guanosine triphosphatase-activating proteins (RasGAPs) mediate the inactivation of Ras proteins.
  • Ten distinct RasGAPs have been identified, exhibiting overlapping tissue distribution.

Purpose of the Study:

  • To discuss recent advances in understanding the functions of RasGAPs.
  • To highlight the critical, nonredundant roles of individual RasGAPs.
  • To explore the involvement of RasGAPs in maintaining tissue integrity and regulating disease.

Main Methods:

  • Review of genetic analyses in mouse and human studies.
  • Analysis of tissue distribution patterns of different RasGAPs.
  • Integration of findings on RasGAP function in homeostasis and disease.

Main Results:

  • Genetic analyses demonstrate that despite overlapping expression, individual RasGAPs have essential, nonredundant functions.
  • RasGAPs play critical roles in maintaining tissue homeostasis.
  • Dysregulation of RasGAP function is implicated in various disease processes.

Conclusions:

  • RasGAPs are vital regulators of Ras signaling, essential for tissue integrity.
  • Understanding the specific functions of each RasGAP is crucial for deciphering their roles in health and disease.
  • Further research into RasGAP biology promises insights into therapeutic strategies for diseases involving Ras pathway dysregulation.

More Related Videos

Comparing the Affinity of GTPase-binding Proteins using Competition Assays10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates

Published on: March 31, 2012

Related Concept Videos

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:
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...
GTPases and their Regulation02:14

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, also known...
GTPases and their Regulation02:14

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, also known...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
Rab Proteins01:14

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...