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

Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

2.1K
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...
2.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.9K
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,...
5.9K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

2.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
2.8K
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

2.3K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
2.3K
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

2.4K
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.4K
The Two-State Receptor Model01:29

The Two-State Receptor Model

2.1K
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
2.1K

You might also read

Related Articles

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

Sort by
Same author

De Novo Discovery of Prenylated Macrocyclic Peptide Ligands.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

<i>De Novo</i> Boronic Acid-Containing Macrocyclic Peptides That Selectively Bind a Sialylated <i>N</i>-Glycan.

Journal of the American Chemical Society·2026
Same author

Post-Translational Aldehyde-Mediated Backbone Alkylation Enables Constrained α-Amino-γ-Lactam Motifs in mRNA Display.

Journal of the American Chemical Society·2026
Same author

A RaPID Macrocyclic Peptide Inhibitor of ROR1/2 Strongly Reduces Proliferation of Diffuse Intrinsic Pontine Glioma Cells.

ACS chemical biology·2026
Same author

Development and structure-guided characterization of a novel ACE2-binding macrocyclic peptide.

Journal of structural biology: X·2026
Same author

The Alteromonas macleodii ribosome enables consecutive incorporation of bulky D-amino acids into peptides.

Nucleic acids research·2026

Related Experiment Video

Updated: Aug 31, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K

De novo Fc-based receptor dimerizers differentially modulate PlexinB1 function.

Nozomi Sugano-Nakamura1, Kyoko Matoba1, Mika Hirose1

  • 1Laboratory for Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Osaka, Japan.

Structure (London, England : 1993)
|August 18, 2022
PubMed
Summary

Researchers engineered novel peptide-based dimerizers for PlexinB1 (PlxnB1) receptor. These agents effectively modulate PlxnB1 signaling by inducing specific dimer conformations, offering potential therapeutic strategies.

Keywords:
Fcantibody surrogatecyclic peptidenegative stain EMplexinreceptor agonistreceptor antagonistreceptor dimerizationsemaphorinsignal transduction

More Related Videos

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM
12:42

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM

Published on: December 22, 2015

10.0K
A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
06:56

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

13.9K

Related Experiment Videos

Last Updated: Aug 31, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
14:02

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

Published on: April 9, 2018

8.6K
Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM
12:42

Photoactivated Localization Microscopy with Bimolecular Fluorescence Complementation BiFC-PALM

Published on: December 22, 2015

10.0K
A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
06:56

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

13.9K

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Engineering

Background:

  • Single-pass transmembrane receptor signaling relies on ligand-induced dimer formation with specific conformations.
  • Bivalent binders can modulate receptor function by altering dimer conformations, but designing them is challenging.

Purpose of the Study:

  • To generate antagonistic and agonistic receptor dimerizers targeting PlexinB1 (PlxnB1), a receptor for semaphorin 4D (Sema4D).
  • To investigate the structure-function relationship of these engineered dimerizers in modulating PlxnB1 signaling.

Main Methods:

  • Grafting two distinct PlxnB1-binding peptides onto a human immunoglobulin G1 (IgG1) Fc protein.
  • Assessing the function-modulating activity of the resulting peptide-Fc variants.
  • Conducting structural analysis of peptide-PlxnB1 complexes.

Main Results:

  • Engineered peptide-Fc variants demonstrated function-modulating activity in the nanomolar concentration range.
  • Activity was dependent on the specific peptide and its grafting site on the Fc protein.
  • Agonistic Fc induced a face-to-face PlxnB1 dimer conformation, similar to Sema4D.
  • Antagonistic Fc induced a signaling-incompetent PlxnB1 dimer conformation.

Conclusions:

  • Receptor orientation within the dimer is a primary determinant of plexin activation.
  • Engineered bivalent binders can effectively control receptor signaling by dictating dimer conformation.
  • This approach provides a versatile platform for developing targeted therapeutics for plexin-mediated pathways.