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Related Concept Videos

Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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...

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Related Experiment Video

Updated: May 16, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
07:08

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

Temperature and lipid composition differentially regulate KRAS assemblies on membranes.

Ji Kang1, Elena Scott1, Sangho D Yun1

  • 1Department of Chemistry, Texas A&M University, College Station, TX 77843, USA. ALaganowsky@chem.tamu.edu.

Chemical Communications (Cambridge, England)
|May 14, 2026
PubMed
Summary
This summary is machine-generated.

RAS GTPases are key signaling proteins. We found KRAS protein dimerization increases with temperature, unlike NRAS, revealing specific membrane organization mechanisms.

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Area of Science:

  • Molecular biology
  • Cellular signaling
  • Biophysics

Background:

  • RAS GTPases are crucial regulators of cellular signaling pathways.
  • The oligomerization of RAS proteins on cell membranes is essential for their function.
  • Factors influencing RAS GTPase membrane organization and dimerization are not fully understood.

Purpose of the Study:

  • To investigate the factors controlling RAS GTPase oligomerization on cell membranes.
  • To determine the specific mechanisms governing KRAS and NRAS dimerization.
  • To elucidate the role of lipids and temperature in RAS protein assembly.

Main Methods:

  • Variable-temperature native mass spectrometry was employed to analyze protein complexes.
  • NanoBiT assays were utilized to measure KRAS and NRAS dimerization in situ.
  • Lipid composition and temperature were systematically varied to assess their impact.

Main Results:

  • KRAS dimerization was found to be dependent on both lipid composition and temperature.
  • Increased temperatures led to enhanced KRAS protein assembly.
  • NRAS dimerization remained unaffected by temperature variations, suggesting isoform-specific regulation.
  • Entropy-driven assembly mechanisms were indicated for KRAS.

Conclusions:

  • Lipid and temperature are critical determinants of KRAS dimerization and membrane organization.
  • RAS GTPase function is modulated by distinct, isoform-specific mechanisms of membrane assembly.
  • This study provides new insights into the regulation of RAS signaling pathways at the molecular level.