ArticleThe Journal of biological chemistry2012
Structural analysis of smooth muscle tropomyosin α and β isoforms.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Tropomyosin micelles are the major components contributing to the white colour of boiled shellfish soups.Scientific reports · 2022Article
- Nanopore sequencing reveals full-length Tropomyosin 1 isoforms and their regulation by RNA-binding proteins during rat heart development.Journal of cellular and molecular medicine · 2021Article
- M8R tropomyosin mutation disrupts actin binding and filament regulation: The beginning affects the middle and end.The Journal of biological chemistry · 2020Article
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Docking Troponin T onto the Tropomyosin Overlapping Domain of Thin Filaments.Biophysical journal · 2020Article
- Article
- Tropomyosin isoforms differentially affect muscle contractility in the head and body regions of the nematode Caenorhabditis elegans.Molecular biology of the cell · 2018Article
- Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H.Protein science : a publication of the Protein Society · 2018Article
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- Binding of smoothelin-like 1 to tropomyosin and calmodulin is mutually exclusive and regulated by phosphorylation.BMC biochemistry · 2017Article
- ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils.Scientific reports · 2017Article
- Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.Journal of muscle research and cell motility · 2015Article
- Direct observation of tropomyosin binding to actin filaments.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Article
- Tropomyosin dynamics.Journal of muscle research and cell motility · 2014Review
- The structural dynamics of α-tropomyosin on F-actin shape the overlap complex between adjacent tropomyosin molecules.Archives of biochemistry and biophysics · 2014Article
- Structure and flexibility of the tropomyosin overlap junction.Biochemical and biophysical research communications · 2014Article
- Molecular mechanical differences between isoforms of contractile actin in the presence of isoforms of smooth muscle tropomyosin.PLoS computational biology · 2013Article
- Tropomodulins and tropomyosins: working as a team.Journal of muscle research and cell motility · 2013Review
- Novel deletion of lysine 7 expands the clinical, histopathological and genetic spectrum of TPM2-related myopathies.Brain : a journal of neurology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
A large number of tropomyosin (Tm) isoforms function as gatekeepers of the actin filament, controlling the spatiotemporal access of actin-binding proteins to specialized actin networks. Residues ∼40-80 vary significantly among Tm isoforms, but the impact of sequence variation on Tm structure and interactions with actin is poorly understood, because structural studies have focused on skeletal muscle Tmα. We describe structures of N-terminal fragments of smooth muscle Tmα and Tmβ (sm-Tmα and sm-Tmβ). The 2.0-Å structure of sm-Tmα81 (81-aa) resembles that of skeletal Tmα, displaying a similar super-helical twist matching the contours of the actin filament. The 1.8-Å structure of sm-Tmα98 (98-aa) unexpectedly reveals an antiparallel coiled coil, with the two chains staggered by only 4 amino acids and displaying hydrophobic core interactions similar to those of the parallel dimer. In contrast, the 2.5-Å structure of sm-Tmβ98, containing Gly-Ala-Ser at the N terminus to mimic acetylation, reveals a parallel coiled coil. None of the structures contains coiled-coil stabilizing elements, favoring the formation of head-to-tail overlap complexes in four of five crystallographically independent parallel dimers. These complexes show similarly arranged 4-helix bundles stabilized by hydrophobic interactions, but the extent of the overlap varies between sm-Tmβ98 and sm-Tmα81 from 2 to 3 helical turns. The formation of overlap complexes thus appears to be an intrinsic property of the Tm coiled coil, with the specific nature of hydrophobic contacts determining the extent of the overlap. Overall, the results suggest that sequence variation among Tm isoforms has a limited effect on actin binding but could determine its gatekeeper function.
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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.