ArticleJournal of proteome research2011
Quantitative analysis of cohesin complex stoichiometry and SMC3 modification-dependent protein interactions.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- The physical chemistry of interphase loop extrusion.Cell genomics · 2026Article
- Quartet protein reference materials and datasets for multi-platform assessment of label-free proteomics.Genome biology · 2023Article
- It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022Review
- Application of targeted mass spectrometry in bottom-up proteomics for systems biology research.Journal of proteomics · 2018Review
- A reference peptide database for proteome quantification based on experimental mass spectrum response curves.Bioinformatics (Oxford, England) · 2018Article
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- Article
- Revealing Higher Order Protein Structure Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Choice of LC-MS methods for the absolute quantification of drug-metabolizing enzymes and transporters in human tissue: a comparative cost analysis.The AAPS journal · 2015Article
- Studying macromolecular complex stoichiometries by peptide-based mass spectrometry.Proteomics · 2015Review
- Biomarkers in Alzheimer's disease analysis by mass spectrometry-based proteomics.International journal of molecular sciences · 2014Review
- Absolute quantification of selected proteins in the human osteoarthritic secretome.International journal of molecular sciences · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Cohesin is a protein complex that plays an essential role in pairing replicated sister chromatids during cell division. The vertebrate cohesin complex consists of four core components including structure maintenance of chromosomes proteins SMC1 and SMC3, RAD21, and SA2/SA1. Extensive research suggests that cohesin traps the sister chromatids by a V-shaped SMC1/SMC3 heterodimer bound to the RAD21 protein that closes the ring. Accordingly, the single "ring" model proposes that two sister chromatids are trapped in a single ring that is composed of one molecule each of the 4 subunits. However, evidence also exists for alternative models. The hand-cuff model suggests that each sister chromatid is trapped individually by two rings that are joined through the shared SA1/SA2 subunit. We report here the determination of cohesin subunit stoichiometry of endogenous cohesin complex by quantitative mass spectrometry. Using qConCAT-based isotope labeling, we show that the cohesin core complex contains equimolar of the 4 core components, suggesting that each cohesin ring is closed by one SA1/SA2 molecule. Furthermore, we applied this strategy to quantify post-translational modification-dependent cohesin interactions. We demonstrate that quantitative mass spectrometry is a powerful tool for measuring stoichiometry of endogenous protein core complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.