Related Experiment Video

Updated: Apr 16, 2026

RhoC GTPase Activation Assay
09:58

RhoC GTPase Activation Assay

Published on: August 22, 2010

13.2K

Ral GTPases: crucial mediators of exocytosis and tumourigenesis

Ryutaro Shirakawa1, Hisanori Horiuchi2

  • 1Department of Molecular and Cellular Biology, Institute of Development, Aging, and Cancer, Tohoku University, Seiryo-machi 4-1, Aoba-ku, Sendai 980-8575, Japan shirakawa@idac.tohoku.ac.jp.

Journal of Biochemistry
|March 22, 2015
PubMed

Insights

Ral guanine nucleotide-binding proteins (GTPases) are crucial in cell functions and cancer development. Targeting Ral GTPase signaling pathways offers a promising strategy for human cancer treatment.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • Ral guanine nucleotide-binding proteins (GTPases), specifically RalA and RalB, are key components of the Ras superfamily.
  • These GTPases play critical roles in diverse cellular processes, including exocyst-mediated exocytosis.

Purpose of the Study:

  • To review recent advancements in the study of Ral GTPases.
  • To highlight the involvement of Ral GTPases in human cancer and their potential as therapeutic targets.

Main Methods:

  • Literature review of research on Ral GTPases over the past 25 years.
  • Analysis of studies investigating the role of Ral GTPases in cellular functions and tumorigenesis.

Main Results:

  • Aberrant activation of Ral GTPases is a significant factor in Ras-induced human tumorigenesis.
  • Ral signaling pathways are increasingly recognized as potential therapeutic targets for cancer treatment.

Conclusions:

  • Ral GTPases are essential regulators of cellular activities.
  • Targeting Ral GTPase pathways presents a promising avenue for developing novel cancer therapies.
Keywords:
RalRasexocystexocytosistumourigenesis

More Related Videos

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein GST-RhoAG17A from Epithelial Cell Lysates

Published on: March 31, 2012

17.0K
Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells10:27

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

Published on: March 9, 2012

11.3K

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:
5.8K
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,...
10.3K
GTPases and their Regulation02:14

GTPases and their Regulation

3.3K
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...
7.6K
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.
3.8K
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...
12.6K