ArticleBiochimica et biophysica acta2016
Localization of the binding interface between leiomodin-2 and α-tropomyosin.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 22 citations in OpenAlex.
- Mechanism of actin thin filament pointed-end elongation by leiomodin.Nature communications · 2026Article
- Localization and functional exploration of leiomodin-2's C-terminal binding sites.Biochimica et biophysica acta. Proteins and proteomics · 2026Article
- N-Terminal Actin-Binding Site of Lmod2 Promotes Controlled Pointed End Elongation.Circulation research · 2026Article
- Prediction and biological significance of small changes in binding of leiomodin to tropomyosin.The Journal of general physiology · 2025Article
- Leiomodin 2 neonatal dilated cardiomyopathy mutation results in altered actin gene signatures and cardiomyocyte dysfunction.NPJ Regenerative medicine · 2024Article
- Case report: cosegregation of a TPM1 in-frame deletion (p.Lys7del) with familial non-compaction cardiomyopathy (NCCM).Clinical research in cardiology : official journal of the German Cardiac Society · 2024Article
- Nuclear Magnetic Resonance-Guided Structural Analysis of Moderate-Affinity Protein Complexes with Intrinsically Disordered Polypeptides.Methods in molecular biology (Clifton, N.J.) · 2023Article
- CaProtein science : a publication of the Protein Society · 2022Article
- CAP2 is a regulator of actin pointed end dynamics and myofibrillogenesis in cardiac muscle.Communications biology · 2021Article
- Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021Article
- Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.PLoS biology · 2020Article
- Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.Journal of muscle research and cell motility · 2020Review
- Effects of cardiomyopathy-linked mutations K15N and R21H in tropomyosin on thin-filament regulation and pointed-end dynamics.Molecular biology of the cell · 2019Article
- Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H.Protein science : a publication of the Protein Society · 2018Article
- Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin.Archives of biochemistry and biophysics · 2018Article
- The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Archives of biochemistry and biophysics · 2017Article
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.PloS one · 2017Article
- The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.Molecular biology of the cell · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The development of some familial dilated cardiomyopathies (DCM) correlates with the presence of mutations in proteins that regulate the organization and function of thin filaments in cardiac muscle cells. Harmful effects of some mutations might be caused by disruption of yet uncharacterized protein-protein interactions. We used nuclear magnetic resonance spectroscopy to localize the region of striated muscle α-tropomyosin (Tpm1.1) that interacts with leiomodin-2 (Lmod2), a member of tropomodulin (Tmod) family of actin-binding proteins. We found that 21 N-terminal residues of Tpm1.1 are involved in interactions with residues 7-41 of Lmod2. The K15N mutation in Tpm1.1, known to be associated with familial DCM, is located within the newly identified Lmod2 binding site of Tpm1.1. We studied the effect of this mutation on binding Lmod2 and Tmod1. The mutation reduced binding affinity for both Lmod2 and Tmod1, which are responsible for correct lengths of thin filaments. The effect of the K15N mutation on Tpm1.1 binding to Lmod2 and Tmod1 provides a molecular rationale for the development of familial DCM.
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