Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Ras Gene02:38

The Ras Gene

7.4K
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...
7.4K
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

5.5K
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:
5.5K
Lipids as Anchors01:32

Lipids as Anchors

7.6K
In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...
7.6K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

8.7K
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...
8.7K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

5.7K
The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
5.7K
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

19.6K
Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
19.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Glycosphingolipids regulate phosphatidylserine transport machinery that operates at ER-PM contact sites.

Nature communications·2026
Same author

DIRAS3-derived cyclic peptides disrupt KRAS-RAF interaction and KRAS nanoclustering, suppressing KRAS-driven pancreatic and ovarian tumors.

iScience·2025
Same author

Terraforming the KRAS lipid landscape.

Nature chemical biology·2025
Same author

MTMR regulates KRAS function by controlling plasma membrane levels of phospholipids.

The Journal of cell biology·2025
Same author

Differential Lipid Binding Specificities of RAP1A and RAP1B are Encoded by the Amino Acid Sequence of the Membrane Anchors.

Journal of the American Chemical Society·2024
Same author

MTMR regulates KRAS function by controlling plasma membrane levels of phospholipids.

bioRxiv : the preprint server for biology·2024
Same journal

Traffic Light Commentary-Src in the Upside Down: A Kinase Turned Inside Out.

Traffic (Copenhagen, Denmark)·2026
Same journal

Integrating Lateral Super-Resolution and Axial Progression Reveals Distinct Clathrin Pit Formation Pathways.

Traffic (Copenhagen, Denmark)·2026
Same journal

A Quarter Century of EHD Protein Research: From Endosomal Recycling to Ciliopathies.

Traffic (Copenhagen, Denmark)·2026
Same journal

Mechanistic Insight Into Clathrin-Mediated Endocytosis in Plants.

Traffic (Copenhagen, Denmark)·2026
Same journal

Clathrin-Mediated Endocytosis in Plants: Historical to Modern Advances.

Traffic (Copenhagen, Denmark)·2026
Same journal

A Toolbox for Quantifying Nuclear and Nucleolar Protein Accumulation Using NLS and NoLS Fusion Reporters.

Traffic (Copenhagen, Denmark)·2026
See all related articles

Related Experiment Video

Updated: Feb 19, 2026

Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans
08:12

Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans

Published on: October 5, 2020

3.4K

Deciphering lipid codes: K-Ras as a paradigm.

Yong Zhou1, John F Hancock1

  • 1Department of Integrative Biology and Pharmacology, McGovern Medical School, University of Texas Health Science Center at Houston, 6431, Fannin Street, Houston, TX.

Traffic (Copenhagen, Denmark)
|November 10, 2017
PubMed
Summary
This summary is machine-generated.

Cell membranes are complex lipid environments. This review explores how K-Ras protein interactions with specific membrane lipids regulate cell signaling and function.

Keywords:
K-Raslipid anchoredphosphatidylserineplasma membranepolybasic domainsmall GTPases

More Related Videos

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

6.1K
Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy
10:59

Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy

Published on: May 28, 2021

4.8K

Related Experiment Videos

Last Updated: Feb 19, 2026

Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans
08:12

Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans

Published on: October 5, 2020

3.4K
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

6.1K
Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy
10:59

Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy

Published on: May 28, 2021

4.8K

Area of Science:

  • Cell biology
  • Biophysics
  • Molecular biology

Background:

  • The cell plasma membrane (PM) is a dynamic and heterogeneous lipid environment.
  • While in vitro biophysical processes of lipid segregation are known, biological roles of PM lipid heterogeneity remain unclear.
  • How membrane proteins exploit transient lipid clustering to regulate function is of significant interest.

Purpose of the Study:

  • To explore how the C-terminal membrane-anchoring domain of K-Ras mediates selective lipid sorting on the PM.
  • To discuss how this lipid specificity influences K-Ras signal transmission and cellular function.

Main Methods:

  • Review of existing literature on K-Ras structure, function, and membrane interactions.
  • Analysis of biophysical principles governing lipid-protein interactions in the plasma membrane.
  • Integration of knowledge on K-Ras signaling pathways.

Main Results:

  • The K-Ras C-terminal domain, featuring a polybasic region and farnesyl anchor, acts as a complex code for selective lipid sorting.
  • Specific lipid interactions mediated by K-Ras's anchoring domain are crucial for its function.
  • Transient spatial clustering of PM lipids is potentially utilized by K-Ras to regulate its signaling.

Conclusions:

  • K-Ras exhibits remarkable specificity in sorting lipids on the plasma membrane via its unique anchoring domain.
  • This lipid-sorting mechanism is critical for modulating K-Ras signal transmission and biological activity.
  • Understanding these lipid-protein interactions offers insights into regulating K-Ras-driven cellular processes.