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Related Concept Videos

Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

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%...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

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 produces two-second...
Synthesis of Phosphatidylcholine in the ER Membrane01:27

Synthesis of Phosphatidylcholine in the ER Membrane

The ER synthesizes lipids for building cell membranes and performing cellular functions such as energy storage and signaling. The lipid synthesis machinery embedded in the ER membrane primarily collects all reactants from the cytosol. Following synthesis, the secretory pathway and the ER contact sites distribute these lipids to other cellular organelles. Additionally, the energy-rich triacylglycerides are transported from the ER via lipid droplets.
The major components of all eukaryotic cell...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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.
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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Related Experiment Video

Updated: Jul 2, 2026

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
18:25

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

The domain responsible for sphingomyelin synthase (SMS) activity.

Calvin Yeang1, Shweta Varshney, Renxiao Wang

  • 1Department of Anatomy and Cell Biology, SUNY Downstate Medical Center, USA.

Biochimica Et Biophysica Acta
|August 13, 2008
PubMed
Summary

Sphingomyelin synthase (SMS) regulates lipid metabolism and cell signaling. Mutating key amino acids in SMS1 and SMS2 inactivated the enzyme, offering potential for new disease treatments.

More Related Videos

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
08:53

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species

Published on: May 7, 2018

A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors
12:27

A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors

Published on: June 8, 2022

Related Experiment Videos

Last Updated: Jul 2, 2026

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds
18:25

Live Imaging Assay for Assessing the Roles of Ca2+ and Sphingomyelinase in the Repair of Pore-forming Toxin Wounds

Published on: August 25, 2013

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
08:53

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species

Published on: May 7, 2018

A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors
12:27

A Pipeline to Investigate the Structures and Signaling Pathways of Sphingosine 1-Phosphate Receptors

Published on: June 8, 2022

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Sphingomyelin synthase (SMS) is crucial in sphingomyelin (SM), ceramide, and diacylglycerol (DAG) metabolism.
  • SMS regulates lipid messengers involved in cell survival and apoptosis.
  • Two isoforms, SMS1 and SMS2, exist and share conserved catalytic residues.

Purpose of the Study:

  • To investigate the functional roles of conserved amino acids in SMS1 and SMS2.
  • To identify domains responsible for the cellular distribution of SMS isoforms.
  • To provide insights for drug development targeting SMS in disease.

Main Methods:

  • Site-directed mutagenesis of conserved amino acids in SMS1 and SMS2.
  • Assessment of enzyme activity post-mutation.
  • Analysis of cellular distribution of wild-type and mutant SMS.
  • Homology modeling of SMS1 and SMS2.

Main Results:

  • Each point mutation in the conserved histidines and aspartic acid abolished SMS activity.
  • Mutations did not alter the cellular distribution of SMS1 or SMS2.
  • Domains responsible for cellular localization were identified.

Conclusions:

  • Conserved residues are essential for SMS catalytic activity but not for cellular localization.
  • Understanding SMS function and distribution is vital for disease regulation.
  • Findings support the development of SMS-targeted therapeutics.