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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:
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...
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...
Rab Cascades01:25

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.
Cell Polarization by Rho Proteins01:21

Cell Polarization by Rho Proteins

Cell polarity is the asymmetric distribution of cellular and membrane components, making one side of the cell different from the other. This polarity is essential to many processes such as embryogenesis, axon migration, glucose transport across epithelial cells, and directional cell migration. A migrating cell responds to intracellular or extracellular signals via molecular cascades that reorganize the actin cytoskeleton to establish this polarity. In these cells, the Rho family proteins Cdc42,...
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...

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p190RhoGAP has cellular RacGAP activity regulated by a polybasic region.

Magdolna Lévay1, Balázs Bartos, Erzsébet Ligeti

  • 1Department of Physiology, Semmelweis University, Budapest, Hungary.

Cellular Signalling
|March 19, 2013
PubMed
Summary
This summary is machine-generated.

p190RhoGAP protein demonstrates significant GTPase-activating protein (GAP) activity towards Rac in cellular environments, not just in vitro. This finding reveals a more intricate role for p190RhoGAP in regulating cellular signaling pathways.

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Published on: January 16, 2017

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells
10:27

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

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Published on: March 31, 2012

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • p190RhoGAP is a GTPase-activating protein (GAP) regulating actin cytoskeleton dynamics.
  • Its GAP domain activates Rho family GTPases in vitro, but cellular activity, particularly towards Rac, is less understood.
  • Previous work indicated inverse regulation of RacGAP and RhoGAP activities by a polybasic region.

Purpose of the Study:

  • To investigate and provide evidence for the cellular RacGAP activity of p190RhoGAP.
  • To elucidate the role of the polybasic region in modulating p190RhoGAP's activity towards Rac and RhoA.
  • To understand the complex role of p190RhoGAP in Rac-Rho antagonism.

Main Methods:

  • Cellular assays to assess GTPase-activating protein activity.
  • Mutagenesis studies focusing on the polybasic region adjacent to the GAP domain.
  • Analysis of p190RhoGAP's effects on Rho and Rac GTPase levels in cells.

Main Results:

  • p190RhoGAP exhibits significant GTPase-activating protein activity towards Rac within the cell.
  • The polybasic region is essential for the cellular RacGAP activity of p190RhoGAP.
  • The same polybasic region inhibits the RhoGAP activity of p190RhoGAP.
  • p190RhoGAP's activity is inversely regulated, showing distinct cellular roles for RacGAP and RhoGAP functions.

Conclusions:

  • p190RhoGAP possesses direct and significant cellular GTPase-activating protein activity towards Rac.
  • The polybasic region acts as a crucial regulatory element, enabling Rac-specific activity while inhibiting RhoA activity.
  • p190RhoGAP plays a more complex role in mediating Rac-Rho antagonism than previously recognized.