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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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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...
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Membrane Fluidity01:23

Membrane Fluidity

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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.
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Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

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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...
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Related Experiment Video

Updated: Sep 15, 2025

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

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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 92831, USA.

Cell Stress & Chaperones
|July 13, 2025
PubMed
Summary

Heat shock increases phosphatidylserine (PS) levels, driving the translocation of HSPA1A protein to the plasma membrane. Inhibiting PS synthesis blocks this movement, revealing PS as a key regulator of HSPA1A

Keywords:
Chaperone traffickingLipidomicsMembrane lipid remodelingProtein-lipid interactionsStress response

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Heat shock protein 1A (HSPA1A) is vital for cell survival and can move to the plasma membrane (PM) in stressed and cancer cells.
  • PM-localized HSPA1A correlates with aggressive cancers and resistance to therapy, 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 plasma membrane during heat stress.
  • To determine if heat-induced alterations in PS levels are the critical factor for HSPA1A's membrane localization.

Main Methods:

  • Pharmacological inhibition and RNA interference were used to target PS synthesis.
  • Confocal microscopy, lipidomics, and western blotting were employed to analyze HSPA1A localization and PS levels.
  • PS-specific biosensors confirmed heat shock-induced changes in PS.

Main Results:

  • Lipidomic analysis and biosensors confirmed a significant, transient increase in PS levels following heat shock.
  • Inhibition of PS synthesis markedly reduced HSPA1A's plasma membrane localization, while cholesterol or fatty acid depletion had minor effects.
  • Changes in PS saturation or elongation did not affect HSPA1A translocation, highlighting the importance of total PS levels.

Conclusions:

  • Phosphatidylserine (PS) is a critical lipid that regulates HSPA1A translocation to the plasma membrane in response to heat stress.
  • This study provides novel insights into lipid-mediated protein trafficking and the cellular stress response.
  • Targeting PS synthesis could offer a therapeutic strategy to inhibit HSPA1A's pro-cancerous membrane localization.