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

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.4K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.4K
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

4.3K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
4.3K
Enlargement of the Plasma Membrane01:22

Enlargement of the Plasma Membrane

1.9K
Cell division and enlargement are processes that require precise control. The control ensures that cell division cannot proceed unless the cell has grown to a specific size. A spherical, dividing cell requires an approximately 1.6X increase in its surface area to double its volume. The secretory pathway also has a significant role in cell membrane enlargement. Secretory vesicles that bud off from the Golgi apparatus and later fuse with the plasma membrane during exocytosis are a major source of...
1.9K
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

11.9K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
11.9K
Membrane Fluidity01:23

Membrane Fluidity

151.1K
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.
151.1K
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

7.2K
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%...
7.2K

You might also read

Related Articles

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

Sort by
Same author

Protein-Lipid Interactions: From Molecular Recognition to Cellular Organization and Disease.

Membranes·2026
Same author

BAGO: A Self-Optimizing Tool for LC-MS Gradient Design in Metabolomics.

Analytical chemistry·2026
Same author

Correction to "Multi-Laboratory Assessment Reveals Variable Ion Species Profiles in Electrospray Ionization Mass Spectrometer".

Journal of the American Society for Mass Spectrometry·2026
Same author

A lipidomics roadmap: from basic research to societal challenges.

Nature communications·2026
Same author

Lipidomic Markers of Tobacco Use and Cessation Associated With Cardiovascular Risk Factors: A Longitudinal Study in American Indian Individuals.

Journal of the American Heart Association·2026
Same author

Multi-Laboratory Assessment Reveals Variable Ion Species Profiles in Electrospray Ionization Mass Spectrometry.

Journal of the American Society for Mass Spectrometry·2026

Related Experiment Video

Updated: Jun 4, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

3.9K

Heat-Induced Phosphatidylserine Changes Drive HSPA1A's Plasma Membrane Localization.

Jensen Low1, Rachel Altman1, Allen Badolian1

  • 1Department of Biological Science, Center for Applied Biotechnology Studies, and Center for Computational and Applied Mathematics, California State University Fullerton, Fullerton, CA, USA.

Biorxiv : the Preprint Server for Biology
|December 23, 2024
PubMed
Summary

Heat shock protein A1A (HSPA1A) moves to the plasma membrane during heat stress, driven by increased phosphatidylserine (PS). Inhibiting PS synthesis blocks this translocation, offering a potential cancer therapy target.

Keywords:
HSPA1A localizationLipidomicsPhosphatidylserinePlasma membraneStress response

More Related Videos

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.2K
Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

9.5K

Related Experiment Videos

Last Updated: Jun 4, 2025

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

3.9K
Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors

Published on: July 17, 2020

6.2K
Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
07:26

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes

Published on: October 15, 2016

9.5K

Area of Science:

  • Molecular Biology
  • Cellular Stress Response
  • Cancer Biology

Background:

  • Heat shock protein A1A (HSPA1A) is vital for cell survival and can localize to the plasma membrane (PM) in stressed and cancer cells.
  • PM-localized HSPA1A (mHSPA1A) correlates with aggressive cancers and treatment resistance, indicating therapeutic potential in blocking its membrane translocation.

Purpose of the Study:

  • To investigate the role of phosphatidylserine (PS) in triggering HSPA1A's translocation to the PM during heat stress.
  • To determine if heat-induced alterations in PS levels are the critical factor for HSPA1A membrane localization.

Main Methods:

  • Pharmacological inhibition and RNA interference (RNAi) targeting PS synthesis.
  • Confocal microscopy, lipidomics, and western blotting to analyze HSPA1A localization and PS levels.
  • PS-specific biosensors to confirm heat-induced PS increase.

Main Results:

  • Heat shock significantly increased PS levels at the plasma membrane, peaking immediately post-stress.
  • Inhibition of PS synthesis, but not cholesterol or fatty acid depletion, markedly reduced HSPA1A's PM localization.
  • The total increase in PS, rather than specific lipid species, was identified as the key regulator of HSPA1A translocation.

Conclusions:

  • Phosphatidylserine (PS) is a critical lipid regulator of HSPA1A membrane translocation in response to heat shock.
  • This study provides novel insights into lipid-mediated protein trafficking and cellular stress responses.
  • Targeting PS synthesis presents a potential therapeutic strategy to inhibit mHSPA1A in cancer.