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

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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,...
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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

You might also read

Related Articles

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

Sort by
Same author

LIPID MAPS: Powering discovery in lipidomics.

Science signaling·2026
Same author

It's time to rethink academic innovation: why technology transfer offices can't do it alone.

Nature biotechnology·2026
Same author

Discovery of a potential CERS2 inhibitor: hit compound identification via structure-based virtual screening and molecular dynamics simulations.

Molecular diversity·2026
Same author

Nucleolin perturbation alters membrane lipid homeostasis.

Molecular omics·2025
Same author

Vaccine-Induced and Hybrid Immunity Against SARS-CoV-2 Variants of Concern in Two Cohorts in Queensland, Australia (2021-2022).

Journal of medical virology·2025
Same author

The Emerging Mycotoxin 2-Amino-14, 16-Dimethyloctadecan-3-ol (AOD) Alters Transcriptional Regulation and Sphingolipid Metabolism and Undergoes <i>N</i>-Acylation by HepG2 Cells.

Toxins·2025

Related Experiment Video

Updated: May 22, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
07:33

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Modulation of ceramide synthase activity via dimerization.

Elad L Laviad1, Samuel Kelly, Alfred H Merrill

  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

The Journal of Biological Chemistry
|April 28, 2012
PubMed
Summary
This summary is machine-generated.

Ceramide synthase (CerS) activity is regulated by dimer formation, influencing sphingolipid acyl chain composition. This post-translational mechanism reveals novel insights into ceramide synthesis regulation.

More Related Videos

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Related Experiment Videos

Last Updated: May 22, 2026

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction
07:33

Lipid Vesicle-mediated Affinity Chromatography using Magnetic Activated Cell Sorting (LIMACS): a Novel Method to Analyze Protein-lipid Interaction

Published on: April 26, 2011

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Sphingolipids, crucial cellular components, are synthesized by ceramide synthases (CerS).
  • CerS enzymes utilize specific acyl-CoAs for N-acylation of sphingoid bases.
  • Tissue-specific sphingolipid acyl chain composition suggests regulation beyond mRNA expression.

Purpose of the Study:

  • To investigate post-translational mechanisms regulating ceramide synthase (CerS) activity.
  • To explore the role of protein interactions, specifically dimer formation, in CerS regulation.
  • To elucidate how CerS dimerization impacts ceramide synthesis and sphingolipid composition.

Main Methods:

  • Western blotting to detect high molecular weight CerS complexes.
  • Co-immunoprecipitation assays to identify CerS interacting partners.
  • Functional assays involving co-expression of wild-type and catalytically inactive CerS variants.
  • Stimulation of ceramide synthesis using curcumin.

Main Results:

  • Ceramide synthase (CerS) activity is modulated by dimer formation.
  • High molecular weight CerS complexes and co-immunoprecipitation confirm CerS dimerization.
  • Dominant-negative inhibition and activity enhancement observed through co-expression of different CerS forms.
  • Curcumin stimulation rapidly induces CerS dimer formation, correlating with increased ceramide synthesis.

Conclusions:

  • Ceramide synthesis is regulated by the formation of CerS dimers.
  • CerS dimerization represents a novel post-translational regulatory mechanism.
  • Interactions between CerS proteins influence the generation of specific ceramide acyl chain compositions and downstream sphingolipids.