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Related Concept Videos

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
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Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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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,...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...

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Updated: May 28, 2026

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation
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Ectodomain structures of Eph receptors.

Juha P Himanen1

  • 1Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA. himanenj@mskcc.org

Seminars in Cell & Developmental Biology
|November 3, 2011
PubMed
Summary

Eph receptors and ephrin ligands mediate cell communication, crucial for development and cancer. Their unique bidirectional signaling and clustering mechanisms, detailed by structural studies, reveal subclass-specific interactions.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Structural Biology

Background:

  • Eph receptors and ephrin ligands are receptor tyrosine kinases critical for cell-cell communication.
  • They regulate key biological processes including axon guidance, potentiation, stem cell development, and cancer progression.
  • Their interaction involves membrane-bound receptors and ligands, forming signaling centers.

Purpose of the Study:

  • To elucidate the structural basis of Eph receptor and ephrin ligand interactions.
  • To understand the formation of higher-order Eph/ephrin clusters and their role in initiating signaling.
  • To define the molecular determinants of subclass specificity within the Eph/ephrin system.

Main Methods:

  • Analysis of crystal structures and biophysical studies of Eph and ephrin extracellular domains.

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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
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  • Investigation of heterodimer formation and higher-order cluster assembly.
  • Examination of sequence conservation and interacting residues defining subclass specificity.

    • Main Results:

    • Isolated Eph and ephrin domains form high-affinity heterodimers via hydrophobic interactions.
    • These dimers further assemble into higher-order clusters through weaker interactions at cell contact sites.
    • Structural differences in extracellular domains dictate unique partner preferences and subclass specificity.

    Conclusions:

    • Eph/ephrin interaction initiates bidirectional signaling through multimerization into signaling centers.
    • Heterodimerization is essential for initiating signaling, with extracellular domains driving higher-order clustering.
    • Specific residues and architectural arrangements govern the precise subclass interactions of Ephs and ephrins.