ArticlePloS one2015
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Polarized branched Actin modulates cortical mechanics to produce unequal-size daughters during asymmetric division.Nature cell biology · 2023Article
- Structural and signaling proteins in the Z-disk and their role in cardiomyopathies.Frontiers in physiology · 2023Review
- The Role of Z-disc Proteins in Myopathy and Cardiomyopathy.International journal of molecular sciences · 2021Review
- A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2.Nature communications · 2020Article
- Drosophila OTK Is a Glycosaminoglycan-Binding Protein with High Conformational Flexibility.Structure (London, England : 1993) · 2020Article
- Respiratory distress in a 2-month-old infant: Is the primary cause cardiac, pulmonary or both?Respiratory medicine case reports · 2018Article
- When signalling goes wrong: pathogenic variants in structural and signalling proteins causing cardiomyopathies.Journal of muscle research and cell motility · 2017Review
- Filamin actin-binding and titin-binding fulfill distinct functions in Z-disc cohesion.PLoS genetics · 2017Article
- Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains.Scientific reports · 2017Article
- Structural and thermodynamic basis of a frontometaphyseal dysplasia mutation in filamin A.The Journal of biological chemistry · 2017Article
- Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection.Structure (London, England : 1993) · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Filamins (FLNs) are large, multidomain actin cross-linking proteins with diverse functions. Besides regulating the actin cytoskeleton, they serve as important links between the extracellular matrix and the cytoskeleton by binding cell surface receptors, functioning as scaffolds for signaling proteins, and binding several other cytoskeletal proteins that regulate cell adhesion dynamics. Structurally, FLNs are formed of an amino terminal actin-binding domain followed by 24 immunoglobulin-like domains (IgFLNs). Recent studies have demonstrated that myosin-mediated contractile forces can reveal hidden protein binding sites in the domain pairs IgFLNa18-19 and 20-21, enabling FLNs to transduce mechanical signals in cells. The atomic structures of these mechanosensor domain pairs in the resting state are known, as well as the structures of individual IgFLN21 with ligand peptides. However, little experimental data is available on how interacting protein binding deforms the domain pair structures. Here, using small-angle x-ray scattering-based modelling, x-ray crystallography, and NMR, we show that the adaptor protein migfilin-derived peptide-bound structure of IgFLNa20-21 is flexible and adopts distinctive conformations depending on the presence or absence of the interacting peptide. The conformational changes reported here may be common for all peptides and may play a role in the mechanosensor function of the site.
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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.