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Cell-surface Signaling

Cell-surface Signaling

Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.

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Related Experiment Video

Updated: Sep 26, 2025

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome

"Cell Surface Capture" Workflow for Label-Free Quantification of the Cell Surface Proteome

Published on: March 24, 2023

Cell Surface Engineering Enables Surfaceome Profiling.

Zak Vilen^1,2,3, Abigail E Reeves^1,2,3, Timothy R O'Leary¹

¹Department of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, Florida 33458, United States.

ACS Chemical Biology

|April 20, 2022

Summary

This summary is machine-generated.

This study introduces a new method for identifying cell surface proteins (CSPs) using engineered cell surfaces and biotinylation. This technique profiles CSPs in different cell types and states, advancing cell biology research.

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Area of Science:

Cell Biology
Biochemistry
Proteomics

Background:

Cell surface proteins (CSPs) are crucial for cell-environment interactions.
Identifying CSPs in various cellular states is essential for understanding cell biology.
Existing CSP identification methods have limitations.

Purpose of the Study:

To develop and evaluate a novel method for profiling cell surface proteins.
To apply this method to identify CSPs in different mammalian cell lines and states.
To compare the new method with existing CSP labeling strategies.

Main Methods:

Cell surface engineering involving cholesterol lipid group prefunctionalization.
Sortase-catalyzed conjugation of APEX2 ascorbate peroxidase enzyme.
Radical-mediated biotinylation of CSPs using APEX2, biotin-phenol, and H2O2.
Streptavidin-based enrichment and quantitative mass spectrometry analysis.

Main Results:

Successfully profiled cell surface proteins in three mammalian cell lines.
Identified distinct CSPs in adherent versus three-dimensional pancreatic adenocarcinoma cells.
Demonstrated the utility of APEX2 in a 'baitless' manner for CSP capture.

Conclusions:

The described method offers a robust approach for cell surface protein profiling.
This technique enables the characterization of CSPs across different cell types and physiological conditions.
The findings contribute to a deeper understanding of cell surface protein dynamics and functions.