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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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.
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Lipids as Anchors01:32

Lipids as Anchors

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.
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GPI Anchoring of Proteins in the ER Membrane01:29

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Membrane Domains01:18

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Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

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Related Experiment Video

Updated: May 10, 2026

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

Orm proteins integrate multiple signals to maintain sphingolipid homeostasis.

Charulatha Gururaj1, Ross S Federman, Ross Federman

  • 1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.

The Journal of Biological Chemistry
|June 6, 2013
PubMed
Summary

Orm proteins regulate sphingolipid synthesis through phosphorylation. This process is influenced by nutrient levels, endoplasmic reticulum stress, and the TOR signaling pathway, impacting cellular homeostasis.

Keywords:
CalcineurinER StressPhosphorylationSignal TransductionSphingolipidTOR

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Last Updated: May 10, 2026

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Analysis of SCAP N-glycosylation and Trafficking in Human Cells
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Published on: November 8, 2016

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Sphingolipids are essential membrane components and signaling molecules.
  • Serine palmitoyltransferase (SPT) catalyzes the rate-limiting step in sphingolipid synthesis.
  • Orm1 and Orm2 are recently discovered proteins that critically regulate SPT activity.

Purpose of the Study:

  • To elucidate the regulatory mechanisms of sphingolipid synthesis.
  • To investigate the role of Orm proteins, TOR signaling, and ER stress in sphingolipid metabolism.

Main Methods:

  • Analysis of Orm protein phosphorylation in response to sphingolipid intermediates.
  • Investigation of TORC1 and TORC2 involvement in sphingolipid synthesis regulation.
  • Examination of the calcium- and calcineurin-dependent pathway in response to ER stress and lipid dysregulation.

Main Results:

  • Orm protein phosphorylation regulates SPT activity in response to sphingolipid levels.
  • TOR signaling pathways (TORC1 and TORC2) modulate sphingolipid synthesis via Orm phosphorylation.
  • Endoplasmic reticulum stress induces ORM2 transcription through a calcium- and calcineurin-dependent pathway, impacting ER homeostasis.

Conclusions:

  • Orm proteins are key regulators of sphingolipid synthesis, integrating signals from lipid intermediates, nutrient availability, and ER stress.
  • The interplay between SPT, Orm proteins, TOR signaling, and ER stress is crucial for maintaining cellular lipid homeostasis.