ArticleMolecular & cellular proteomics : MCP2014
Elution profile analysis of SDS-induced subcomplexes by quantitative mass spectrometry.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
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- Gene augmentation of LCA5-associated Leber congenital amaurosis ameliorates bulge region defects of the photoreceptor ciliary axoneme.JCI insight · 2023Article
- Cilia-localized GID/CTLH ubiquitin ligase complex regulates protein homeostasis of sonic hedgehog signaling components.Journal of cell science · 2022Article
- Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase.Molecular cell · 2021Article
- The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.Autophagy · 2020Article
- Tagging enhances histochemical and biochemical detection of Ran Binding Protein 9 in vivo and reveals its interaction with Nucleolin.Scientific reports · 2020Article
- Gid10 as an alternative N-recognin of the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The mammalian CTLH complex is an E3 ubiquitin ligase that targets its subunit muskelin for degradation.Scientific reports · 2019Article
- The CTLH Complex in Cancer Cell Plasticity.Journal of oncology · 2019Review
- Scorpins in the DNA Damage Response.International journal of molecular sciences · 2018Review
- Cell signalling pathway regulation by RanBPM: molecular insights and disease implications.Open biology · 2017Review
- An organelle-specific protein landscape identifies novel diseases and molecular mechanisms.Nature communications · 2016Article
- Phospho-proteomic analyses of B-Raf protein complexes reveal new regulatory principles.Oncotarget · 2016Article
- KIAA0556 is a novel ciliary basal body component mutated in Joubert syndrome.Genome biology · 2015Article
- NINL and DZANK1 Co-function in Vesicle Transport and Are Essential for Photoreceptor Development in Zebrafish.PLoS genetics · 2015Article
- Expression of leukemia inhibitory factor in Müller glia cells is regulated by a redox-dependent mRNA stability mechanism.BMC biology · 2015Article
- Quantitative affinity purification mass spectrometry: a versatile technology to study protein-protein interactions.Frontiers in genetics · 2015Review
- Cluap1 is essential for ciliogenesis and photoreceptor maintenance in the vertebrate eye.Investigative ophthalmology & visual science · 2014Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Analyzing the molecular architecture of native multiprotein complexes via biochemical methods has so far been difficult and error prone. Protein complex isolation by affinity purification can define the protein repertoire of a given complex, yet, it remains difficult to gain knowledge of its substructure or modular composition. Here, we introduce SDS concentration gradient induced decomposition of protein complexes coupled to quantitative mass spectrometry and in silico elution profile distance analysis. By applying this new method to a cellular transport module, the IFT/lebercilin complex, we demonstrate its ability to determine modular composition as well as sensitively detect known and novel complex components. We show that the IFT/lebercilin complex can be separated into at least five submodules, the IFT complex A, the IFT complex B, the 14-3-3 protein complex and the CTLH complex, as well as the dynein light chain complex. Furthermore, we identify the protein TULP3 as a potential new member of the IFT complex A and showed that several proteins, classified as IFT complex B-associated, are integral parts of this complex. To further demonstrate EPASIS general applicability, we analyzed the modular substructure of two additional complexes, that of B-RAF and of 14-3-3-ε. The results show, that EPASIS provides a robust as well as sensitive strategy to dissect the substructure of large multiprotein complexes in a highly time- as well as cost-effective manner.
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