Related Experiment Video
Updated: Oct 2, 2025
06:45
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
15.3K
Ras Multimers on the Membrane: Many Ways for a Heart-to-Heart Conversation
E Sila Ozdemir1, Anna M Koester2, Xiaolin Nan1,2
1Cancer Early Detection Advanced Research Center, Knight Cancer Institute, Oregon Health & Science University, 2720 S Moody Ave., Portland, OR 97201, USA.
Genes
|February 25, 2022
Summary
Ras proteins form multimers like dimers and nanoclusters, revealing new insights into Ras biomedicine. Understanding their structure and formation is key to exploring their role in cell biology and disease.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Ras proteins are critical regulators of cellular signaling pathways.
- Aberrant Ras signaling is implicated in numerous human diseases, particularly cancer.
- Recent research highlights the formation of Ras multimers (dimers, nanoclusters) as a significant area of study.
Purpose of the Study:
- To synthesize current knowledge on Ras multimer structure and formation mechanisms.
- To explore the influence of membrane nanodomain composition on Ras multimer assembly.
- To discuss the potential implications of Ras multimers in basic and translational research.
Main Methods:
- Review and synthesis of existing literature on Ras protein structure and function.
- Analysis of studies investigating Ras multimer formation in vitro and in cellular contexts.
- Discussion of biophysical principles governing protein-ligand interactions at membranes.
Main Results:
- Ras multimers, including dimers and nanoclusters, are formed through specific globular (G-) domain interfaces.
- Preliminary understanding of in vitro and in-cell mechanisms regulating Ras multimer formation.
- Hypothesized influence of membrane nanodomain characteristics on multimerization.
Conclusions:
- Ras multimerization represents a novel regulatory mechanism in Ras signaling.
- Further investigation into Ras multimer structure and dynamics is warranted.
- Understanding Ras multimers may offer new therapeutic strategies for Ras-driven diseases.
Related Concept Videos
01:30Assembly of Signaling Complexes
6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
6.0K
01:09Multi-pass Transmembrane Proteins and β-barrels
5.7K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.7K
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
11.5K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
11.5K
01:32Types of Signaling Molecules
11.2K
In multicellular organisms, many molecules transmit signals between cells to pass information. These signals vary in complexity and include small peptides, nucleotides, steroids, fatty acid derivatives, and dissolved gases such as nitric oxide. Some signaling molecules diffuse through the plasma membrane to act locally between neighboring cells or travel long distances. Others remain attached to the cell surface, transmitting information to other cells only when they make contact. In some...
11.2K
01:07MAPK Signaling Cascades
6.4K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
6.4K
01:25Single-pass Transmembrane Proteins
5.5K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
5.5K