Related Experiment Video

Updated: Apr 19, 2026

A BW Reporter System for Studying Receptor-Ligand Interactions
06:05

A BW Reporter System for Studying Receptor-Ligand Interactions

Published on: January 7, 2019

8.3K

Esophageal cancer-related gene-4 (ECRG4) interactions with the innate immunity receptor complex

Sonia Podvin1, Xitong Dang, Morgan Meads

  • 1Division of Trauma, Surgical Critical Care, Burns, and Acute Care Surgery, Department of Surgery, University of California, San Diego, San Diego, CA, USA.

Inflammation Research : Official Journal of the European Histamine Research Society ... [Et Al.]
|December 17, 2014
PubMed
Abstract

Insights

Esophageal cancer-related gene-4 (ECRG4) interacts with the Toll-like receptor 4 (TLR4)-MD2-CD14 complex on human leukocytes. This interaction suggests ECRG4 plays a role in inflammation via cell surface activation.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The c2orf40 gene encodes esophageal cancer-related gene-4 (ECRG4), a tumor suppressor with dual inflammatory roles.
  • ECRG4's activity is modulated by cell surface processing, suggesting interactions with cell surface receptors.

Purpose of the Study:

  • To investigate the physical and functional association between ECRG4 and the innate immunity receptor complex.
  • To elucidate the role of ECRG4 in immune cell interactions and inflammatory signaling.

Main Methods:

  • Flow cytometry, immunohistochemistry, confocal microscopy, and co-immunoprecipitation were used to assess ECRG4 interactions.
  • Phage display was employed for ligand targeting to cells expressing the TLR4-MD2-CD14 complex.

Main Results:

  • ECRG4 physically interacts with the TLR4-MD2-CD14 complex on human granulocytes.
  • ECRG4 is expressed on the cell surface of CD14(+) and CD16(+) leukocytes.
  • A processed ECRG4 peptide (ECRG4(133-148)) internalizes via TLR4/CD14/MD2 and modulates inflammation through non-canonical NFκB signaling.

Conclusions:

  • ECRG4 is present on human monocytes and granulocytes, interacting with the innate immunity receptor complex.
  • This interaction supports a role for cell surface ECRG4 activation in inflammatory processes.
  • The study implicates the TLR4-MD2-CD14 complex in ECRG4's mechanism of action during inflammation.

More Related Videos

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 406:56

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4

Published on: March 10, 2018

14.7K
Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells09:04

Activation and Measurement of NLRP3 Inflammasome Activity Using IL-1β in Human Monocyte-derived Dendritic Cells

Published on: May 22, 2014

21.6K

Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
3.3K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
3.0K
Signal Transduction: Overview01:26

Signal Transduction: Overview

Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
13.2K
Allergic Drug Reactions01:27

Allergic Drug Reactions

Allergic reactions related to drugs are hypersensitivity responses driven by the immune system and bear no connection to the drug's therapeutic action. While drugs in isolation do not trigger an immune response, they can interact with endogenous proteins to form antigens. These antigens stimulate lymphocytes to produce antibodies. IgE-type antibodies attach themselves to mast cells. Upon subsequent exposure to the same stimulus, the antigen-antibody interaction is initiated, unleashing...
1.6K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
20.2K
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of...
8.4K