ArticleBiophysical journal2005
Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Interaction of cardiac leiomodin with the native cardiac thin filament.PLoS biology · 2025Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Tmod3 Phosphorylation Mediates AMPK-Dependent GLUT4 Plasma Membrane Insertion in Myoblasts.Frontiers in endocrinology · 2021Article
- Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.PLoS biology · 2020Article
- Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.The Journal of cell biology · 2020Article
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins.Molecules and cells · 2018Review
- Tropomodulin's Actin-Binding Abilities Are Required to Modulate Dendrite Development.Frontiers in molecular neuroscience · 2018Article
- Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Molecular and cellular neurosciences · 2017Review
- The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Archives of biochemistry and biophysics · 2017Article
- Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells.Molecular biology of the cell · 2017Article
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.Molecular biology of the cell · 2016Article
- Tropomyosin-binding properties modulate competition between tropomodulin isoforms.Archives of biochemistry and biophysics · 2016Article
- Tropomodulin isoforms utilize specific binding functions to modulate dendrite development.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Localization of the binding interface between leiomodin-2 and α-tropomyosin.Biochimica et biophysica acta · 2016Article
- How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.Nature communications · 2015Article
- Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.Journal of cell science · 2015Article
- Phosphorylation of tropomodulin1 contributes to the regulation of actin filament architecture in cardiac muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Two families of actin regulatory proteins are the tropomodulins and tropomyosins. Tropomodulin binds to tropomyosin (TM) and to the pointed end of actin filaments and "caps" the pointed end (i.e., inhibits its polymerization and depolymerization). Tropomodulin 1 has two distinct actin-capping regions: a folded C-terminal domain (residues 160-359), which does not bind to TM, and a conserved, N-terminal region, within residues 1-92 that binds TM and requires TM for capping activity. NMR and circular dichroism were used to determine the structure of a peptide containing residues 1-92 of tropomodulin (Tmod1(1-92)) and to define its TM binding site. Tmod1(1-92) is mainly disordered with only one helical region, residues 24-35. This helix forms part of the TM binding domain, residues 1-35, which become more ordered upon binding a peptide containing the N-terminus of an alpha-TM. Mutation of L27 to E or G in the Tmod helix reduces TM affinity. Residues 49-92 are required for capping but do not bind TM. Of these, residues 67-75 have the sequence of an amphipathic helix, but are not helical. Residues 55-62 and 76-92 display negative 1H-15N heteronuclear Overhauser enhancements showing they are flexible. The conformational dynamics of these residues may be important for actin capping activity.
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