ArticleProceedings of the National Academy of Sciences of the United States of America2011
Cysteine shotgun-mass spectrometry (CS-MS) reveals dynamic sequence of protein structure changes within mutant and stressed cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- A shear stress-responsive pathway in monocytes drives cardiopulmonary bypass-induced inflammation via spectrin/RAF1/store-operated calcium entry.Cell reports · 2026Article
- Spectrins: molecular organizers and targets of neurological disorders.Nature reviews. Neuroscience · 2023Review
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
- Cytoskeleton-inspired artificial protein design to enhance polymer network elasticity.Macromolecules · 2020Article
- Article
- Cargo hold and delivery: Ankyrins, spectrins, and their functional patterning of neurons.Cytoskeleton (Hoboken, N.J.) · 2020Review
- Axonal cytomechanics in neuronal development.Journal of biosciences · 2020Review
- Spectrin is a mechanoresponsive protein shaping fusogenic synapse architecture during myoblast fusion.Nature cell biology · 2018Article
- Quantifying forces in cell biology.Nature cell biology · 2017Review
- Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia.Antioxidants & redox signaling · 2017Review
- High content image analysis of focal adhesion-dependent mechanosensitive stem cell differentiation.Integrative biology : quantitative biosciences from nano to macro · 2016Article
- S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding.Cell · 2014Article
- Forced protein unfolding leads to highly elastic and tough protein hydrogels.Nature communications · 2013Article
- Finding the weakest link: exploring integrin-mediated mechanical molecular pathways.Journal of cell science · 2012Review
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Spectrin-based skeleton as an actor in cell signaling.Cellular and molecular life sciences : CMLS · 2012Review
- Native ultrastructure of the red cell cytoskeleton by cryo-electron tomography.Biophysical journal · 2011Article
- Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A.Nature · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Questions of if and when protein structures change within cells pervade biology and include questions of how the cytoskeleton sustains stresses on cells--particularly in mutant versus normal cells. Cysteine shotgun labeling with fluorophores is analyzed here with mass spectrometry of the spectrin-actin membrane skeleton in sheared red blood cell ghosts from normal and diseased mice. Sheared samples are compared to static samples at 37 °C in terms of cell membrane intensity in fluorescence microscopy, separated protein fluorescence, and tryptic peptide modification in liquid chromatography-tandem mass spectrometry (LC-MS/MS). Spectrin labeling proves to be the most sensitive to shear, whereas binding partners ankyrin and actin exhibit shear thresholds in labeling and both the ankyrin-binding membrane protein band 3 and the spectrin-actin stabilizer 4.1R show minimal differential labeling. Cells from 4.1R-null mice differ significantly from normal in the shear-dependent labeling of spectrin, ankyrin, and band 3: Decreased labeling of spectrin reveals less stress on the mutant network as spectrin dissociates from actin. Mapping the stress-dependent labeling kinetics of α- and β-spectrin by LC-MS/MS identifies Cys in these antiparallel chains that are either force-enhanced or force-independent in labeling, with structural analyses indicating the force-enhanced sites are sequestered either in spectrin's triple-helical domains or in interactions with actin or ankyrin. Shear-sensitive sites identified comprehensively here in both spectrin and ankyrin appear consistent with stress relief through forced unfolding followed by cytoskeletal disruption.
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