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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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IP3/DAG Signaling Pathway01:11

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

PI3K/mTOR/AKT Signaling Pathway

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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...
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The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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GPI Anchoring of Proteins in the ER Membrane01:29

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Related Experiment Video

Updated: Nov 28, 2025

Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Elevating PI3P drives select downstream membrane trafficking pathways.

Noah Steinfeld1,2, Vikramjit Lahiri2,3, Anna Morrison2

  • 1Program in Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI 48109.

Molecular Biology of the Cell
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Elevating phosphatidylinositol-3-phosphate (PI3P) can drive or delay cellular pathways. This study shows PI3P is rate-limiting for some processes but slows autophagy, demonstrating dynamic phosphoinositide regulation.

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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Single-molecule Super-resolution Imaging of Phosphatidylinositol 4,5-bisphosphate in the Plasma Membrane with Novel Fluorescent Probes
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Identification of Inositol Phosphate or Phosphoinositide Interacting Proteins by Affinity Chromatography Coupled to Western Blot or Mass Spectrometry
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Phosphoinositide signaling lipids are crucial for cellular functions.
  • Typically, their roles are studied by depletion, with less known about effects of elevation.
  • Stimuli-induced phosphoinositide increases suggest they actively drive cellular pathways.

Purpose of the Study:

  • To investigate the consequences of elevated phosphatidylinositol-3-phosphate (PI3P) levels.
  • To test if increased PI3P drives downstream cellular processes.

Main Methods:

  • Generated hyperactive alleles of yeast phosphatidylinositol 3-kinase, Vps34, to elevate PI3P.
  • Assessed effects on various cellular pathways, including autophagy and vacuole transport.

Main Results:

  • Elevated PI3P drove phosphatidylinositol-3,5-bisphosphate synthesis and retrograde vacuolar transport.
  • PI3P elevation was found to be rate-limiting for these pathways.
  • Conversely, elevated PI3P delayed late stages of autophagy, including autophagosome-vacuole fusion and protein disassembly.

Conclusions:

  • Phosphatidylinositol-3-phosphate (PI3P) levels dynamically regulate distinct downstream pathways.
  • Elevating PI3P can either accelerate or decelerate cellular processes, highlighting its complex regulatory role.
  • Stimulus-induced PI3P increases offer a mechanism for selective regulation of cellular functions.