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

Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze 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,...
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...
Notch Signaling Pathway03:14

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...
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...
Phosphorylation01:02

Phosphorylation

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...

You might also read

Related Articles

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

Sort by
Same author

Evaluating the experiences of Vietnamese university students enrolled in a longitudinal research cohort: a journey mapping approach.

Frontiers in medicine·2026
Same author

Oral Colon-Targeted Lipid Nanoparticles Enhance Upadacitinib Delivery and Efficacy in a Murine Model of Ulcerative Colitis.

International journal of molecular sciences·2026
Same author

Monitoring Biomolecular Changes During Colitis Progression Using Infrared Spectroscopy in Dextran Sodium Sulfate-Treated Mouse Serum.

Journal of biophotonics·2026
Same author

Caregivers' understanding and response to healthcare-associated infections in hospitalised children in Vietnam: a qualitative study.

BMJ paediatrics open·2026
Same author

Expanding the molecular epidemiology of melioidosis in North Central Vietnam.

PLoS neglected tropical diseases·2026
Same author

Harnessing design of experiments and automation significantly improves transient protein production in Chinese hamster ovary cells and accelerates drug discovery.

New biotechnology·2026

Related Experiment Video

Updated: Jun 27, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Ecto-phosphorylation of CD98 regulates cell-cell interactions.

Hang Thi Thu Nguyen1, Guillaume Dalmasso, Yutao Yan

  • 1Division of Digestive Diseases, Department of Medicine, Emory University School of Medicine, Atlanta, Georgia, United States of America. hnguye9@emory.edu

Plos One
|December 10, 2008
PubMed
Summary

Extracellular phosphorylation of CD98 glycoprotein by ecto-protein kinases (ePKs) enhances cell-cell interactions. This ecto-phosphorylation, particularly at specific serine sites, is crucial for CD98

More Related Videos

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy
05:50

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy

Published on: November 1, 2021

Related Experiment Videos

Last Updated: Jun 27, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
10:54

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy
05:50

Measuring Cell-Edge Protrusion Dynamics during Spreading using Live-Cell Microscopy

Published on: November 1, 2021

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ecto-phosphorylation is vital for cellular functions.
  • The CD98 glycoprotein has extracellular phosphorylation sites.
  • CD98 influences cell-cell interactions.

Purpose of the Study:

  • To investigate extracellular signaling via ecto-protein kinases (ePKs) on CD98 ecto-phosphorylation.
  • To determine the role of CD98 ecto-phosphorylation in cell-cell interactions.

Main Methods:

  • In vitro phosphorylation of recombinant CD98 using ePKs from Jurkat cells and casein kinase 2 (CK2).
  • Site-directed mutagenesis (alanine substitutions) to identify phosphorylation sites.
  • Analysis of CD98 ecto-phosphorylation in Caco2-BBE cells.
  • Cell attachment assays to evaluate the impact of CD98 phosphorylation on cell interactions.

Main Results:

  • Recombinant CD98 was phosphorylated by ePKs and CK2 in vitro.
  • Serines-305/307/309 and serines-426/430 were identified as key CK2 phosphorylation sites.
  • CD98 ecto-phosphorylation occurred in Caco2-BBE cells involving ePKs and CK2.
  • Ecto-phosphorylation of CD98 significantly enhanced heterotypic cell-cell interactions.
  • Phosphorylation increased CD98 interaction with cells, promoting attachment and spreading.

Conclusions:

  • Demonstrated ecto-phosphorylation of CD98 by ePKs and its functional significance in cell-cell interactions.
  • Identified a novel mechanism regulating CD98 functions through extracellular phosphorylation.
  • CD98 is a potential therapeutic target for modulating cell-cell interactions.