ArticleBiophysical journal2008
Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 47 citations in OpenAlex.
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- Minimum information guidelines for experiments structurally characterizing intrinsically disordered protein regions.Nature methods · 2023Review
- Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely movingeLife · 2021Article
- Single-particle virology.Biophysical reviews · 2020Review
- Probing Changes in CaMicromachines · 2020Article
- Nucleolin mediates the binding of cancer cells to L-selectin under conditions of lymphodynamic shear stress.American journal of physiology. Cell physiology · 2020Article
- Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017Review
- Twitchin kinase inhibits muscle activity.Molecular biology of the cell · 2017Article
- From genes to protein mechanics on a chip.Nature methods · 2014Article
- Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.Chemical reviews · 2014Review
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Identification of an N-terminal inhibitory extension as the primary mechanosensory regulator of twitchin kinase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.The Journal of biological chemistry · 2011Article
- Cytoskeletal protein kinases: titin and its relations in mechanosensing.Pflugers Archiv : European journal of physiology · 2011Review
- A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 2011Article
- Deconvolution of dynamic mechanical networks.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Optical trapping with high forces reveals unexpected behaviors of prion fibrils.Nature structural & molecular biology · 2010Article
- Substrate elasticity provides mechanical signals for the expansion of hemopoietic stem and progenitor cells.Nature biotechnology · 2010Article
- Extensive and modular intrinsically disordered segments in C. elegans TTN-1 and implications in filament binding, elasticity and oblique striation.Journal of molecular biology · 2010Article
- A LIM-9 (FHL)/SCPL-1 (SCP) complex interacts with the C-terminal protein kinase regions of UNC-89 (obscurin) in Caenorhabditis elegans muscle.Journal of molecular biology · 2009Article
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6 authors at 2 institutions in 1 country.
Funding
Abstract
Myofibril assembly and disassembly are complex processes that regulate overall muscle mass. Titin kinase has been implicated as an initiating catalyst in signaling pathways that ultimately result in myofibril growth. In titin, the kinase domain is in an ideal position to sense mechanical strain that occurs during muscle activity. The enzyme is negatively regulated by intramolecular interactions occurring between the kinase catalytic core and autoinhibitory/regulatory region. Molecular dynamics simulations suggest that human titin kinase acts as a force sensor. However, the precise mechanism(s) resulting in the conformational changes that relieve the kinase of this autoinhibition are unknown. Here we measured the mechanical properties of the kinase domain and flanking Ig/Fn domains of the Caenorhabditis elegans titin-like proteins twitchin and TTN-1 using single-molecule atomic force microscopy. Our results show that these kinase domains have significant mechanical resistance, unfolding at forces similar to those for Ig/Fn beta-sandwich domains (30-150 pN). Further, our atomic force microscopy data is consistent with molecular dynamic simulations, which show that these kinases unfold in a stepwise fashion, first an unwinding of the autoinhibitory region, followed by a two-step unfolding of the catalytic core. These data support the hypothesis that titin kinase may function as an effective force sensor.
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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.