Pooled extracellular receptor-ligand interaction screening using CRISPR activation.

Zheng-Shan Chong; Shuhei Ohnishi; Kosuke Yusa; Gavin J Wright

doi:10.1186/s13059-018-1581-3

Pooled extracellular receptor-ligand interaction screening using CRISPR activation.

Zheng-Shan Chong, Shuhei Ohnishi, Kosuke Yusa, Gavin J Wright

Research output: Contribution to journal › Article › peer-review

Abstract

Extracellular interactions between cell surface receptors are necessary for signaling and adhesion but identifying them remains technically challenging. We describe a cell-based genome-wide approach employing CRISPR activation to identify receptors for a defined ligand. We show receptors for high-affinity antibodies and low-affinity ligands can be unambiguously identified when used in pools or as individual binding probes. We apply this technique to identify ligands for the adhesion G-protein-coupled receptors and show that the Nogo myelin-associated inhibitory proteins are ligands for ADGRB1. This method will enable extracellular receptor-ligand identification on a genome-wide scale.

Original language	English
Article number	205
Number of pages	16
Journal	Genome biology
Volume	19
DOIs	https://doi.org/10.1186/s13059-018-1581-3
Publication status	Published - 26 Nov 2018

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10.1186/s13059-018-1581-3

s13059-018-1581-3
© The Author(s). 2018
Final published version, 2.79 MBLicence: CC BY

Cite this

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title = "Pooled extracellular receptor-ligand interaction screening using CRISPR activation.",

abstract = "Extracellular interactions between cell surface receptors are necessary for signaling and adhesion but identifying them remains technically challenging. We describe a cell-based genome-wide approach employing CRISPR activation to identify receptors for a defined ligand. We show receptors for high-affinity antibodies and low-affinity ligands can be unambiguously identified when used in pools or as individual binding probes. We apply this technique to identify ligands for the adhesion G-protein-coupled receptors and show that the Nogo myelin-associated inhibitory proteins are ligands for ADGRB1. This method will enable extracellular receptor-ligand identification on a genome-wide scale.",

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AB - Extracellular interactions between cell surface receptors are necessary for signaling and adhesion but identifying them remains technically challenging. We describe a cell-based genome-wide approach employing CRISPR activation to identify receptors for a defined ligand. We show receptors for high-affinity antibodies and low-affinity ligands can be unambiguously identified when used in pools or as individual binding probes. We apply this technique to identify ligands for the adhesion G-protein-coupled receptors and show that the Nogo myelin-associated inhibitory proteins are ligands for ADGRB1. This method will enable extracellular receptor-ligand identification on a genome-wide scale.

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