ArticleMolecular & cellular proteomics : MCP2017
Quantitative GTPase Affinity Purification Identifies Rho Family Protein Interaction Partners.
Article in Molecular & cellular proteomics : MCP, 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, 22 citations in OpenAlex.
- GIMAP6 regulates autophagy, immune competence, and inflammation in mice and humans.The Journal of experimental medicine · 2022Article
- Yersinia remodels epigenetic histone modifications in human macrophages.PLoS pathogens · 2021Article
- HPLC method to resolve, identify and quantify guanine nucleotides bound to recombinant ras GTPase.Analytical biochemistry · 2021Article
- GLOBAL AND TARGETED PROFILING OF GTP-BINDING PROTEINS IN BIOLOGICAL SAMPLES BY MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- High Throughput strategies Aimed at Closing the GAP in Our Knowledge of Rho GTPase Signaling.Cells · 2020Review
- Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms.Nature cell biology · 2020Article
- The role of polarisation of circulating tumour cells in cancer metastasis.Cellular and molecular life sciences : CMLS · 2019Review
- In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation.eLife · 2019Article
- Deciphering the Roles of N-Glycans on Collagen-Platelet Interactions.Journal of proteome research · 2019Article
- Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase.Nature communications · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although Rho GTPases are essential molecular switches involved in many cellular processes, an unbiased experimental comparison of their interaction partners was not yet performed. Here, we develop quantitative GTPase affinity purification (qGAP) to systematically identify interaction partners of six Rho GTPases (Cdc42, Rac1, RhoA, RhoB, RhoC, and RhoD), depending on their nucleotide loading state. The method works with cell line or tissue-derived protein lysates in combination with SILAC-based or label-free quantification, respectively. We demonstrate that qGAP identifies known and novel binding partners that can be validated in an independent assay. Our interaction network for six Rho GTPases contains many novel binding partners, reveals highly promiscuous interaction of several effectors, and mirrors evolutionary relationships among Rho GTPases.
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