ArticleMethods in molecular biology (Clifton, N.J.)2017
Single-Step Affinity Purification of ERK Signaling Complexes Using the Streptavidin-Binding Peptide (SBP) Tag.
Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Modular toolkit to facilitate molecular manipulations in mycobacteria.Journal of bacteriology · 2026Article
- ERK inhibits Capicua repressor function via multisite phosphorylation.Journal of cell science · 2026Article
- Hippo pathway and Bonus control developmental cell fate decisions in the Drosophila eye.Developmental cell · 2023Article
- NDR kinase tricornered genetically interacts with Ccm3 and metabolic enzymes in Drosophila melanogaster tracheal development.G3 (Bethesda, Md.) · 2023Article
- Two neuronal peptides encoded from a single transcript regulate mitochondrial complex III ineLife · 2022Article
- Article
- Activation-induced substrate engagement in ERK signaling.Molecular biology of the cell · 2020Article
- Preparation and characterization of a single-domain antibody specific for the porcine epidemic diarrhea virus spike protein.AMB Express · 2019Article
- A Hippo-like Signaling Pathway Controls Tracheal Morphogenesis in Drosophila melanogaster.Developmental cell · 2018Article
- Lgl reduces endosomal vesicle acidification and Notch signaling by promoting the interaction between Vap33 and the V-ATPase complex.Science signaling · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Elucidation of biological functions of signaling proteins is facilitated by studying their protein-protein interaction networks. Affinity purification combined with mass spectrometry (AP-MS) has become a favorite method to study protein complexes. Here we describe a procedure for single-step purification of ERK (Rolled) and associated proteins from Drosophila cultured cells. The use of the streptavidin-binding peptide (SBP) tag allows for a highly efficient isolation of native ERK signaling complexes, which are suitable for subsequent analysis by mass spectrometry. Our analysis of the ERK interactome has identified both known and novel signaling components. This method can be easily adapted for SBP-based purification of protein complexes in any expression system.
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