Affinage

TPM2

Tropomyosin beta chain · UniProt P07951

Length
284 aa
Mass
32.9 kDa
Annotated
2026-06-10
49 papers in source corpus 24 papers cited in narrative 23 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TPM2 encodes beta-tropomyosin, an actin-binding coiled-coil protein that regulates striated muscle contraction by positioning tropomyosin strands on the thin filament and gating Ca2+-dependent transitions between blocked, closed, and open states that permit or inhibit myosin cross-bridge formation (PMID:22084935, PMID:26708479, PMID:38156416). Pathogenic missense and in-frame deletion mutations cluster in actin-binding and head-to-tail polymerization regions and act through several biophysical mechanisms: reduced actin affinity and impaired sarcomeric incorporation (PMID:22084935, PMID:23378224), altered tropomyosin flexibility and azimuthal position on actin (PMID:29196649, PMID:29097206), and shifted equilibrium of the thin filament regulatory state (PMID:26708479, PMID:29792862, PMID:31864708). These changes resolve into two opposing molecular phenotypes — hypercontractile variants that hold tropomyosin near the open position, increase Ca2+ sensitivity, accelerate myosin product release, and stimulate motor activity, versus hypocontractile variants that freeze tropomyosin near the blocked position, reduce Ca2+ sensitivity, and suppress actomyosin ATPase and motility (PMID:33919826, PMID:38156416, PMID:40657867). Beyond steady-state regulation, Tpm2.2 controls thin filament dynamics by inhibiting spontaneous actin polymerization and modulating cofilin-2-mediated filament turnover, with the tropomyosin–troponin complex protecting filaments from disassembly (PMID:42239403). Direct genetic and biochemical evidence establishes TPM2 mutations as a cause of nemaline myopathy, cap disease, distal arthrogryposis, and Sheldon-Hall syndrome (PMID:11738357, PMID:17434307, PMID:19345583, PMID:29097206, PMID:31864708), and disrupted myogenesis is itself a pathomechanism across model organisms (PMID:35579956). Cytoplasmic Tpm2 isoforms perform distinct cytoskeletal roles: they directly bind and inhibit fascin-1-mediated actin bundling (PMID:40887664), regulate cell migration and invasion through actomyosin contractility and ROCK signaling (PMID:29221121), and suppress tumor progression by competing with YAP1 for PDLIM7 to retain YAP1 in the cytoplasm in its inactivated form (PMID:36823643).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2002 Medium

    Established that TPM2 mutations cause human myopathy, framing beta-tropomyosin as a disease gene whose lesions likely act through dimer formation and actin binding.

    Evidence SSCP, sequencing and mutant-allele expression analysis in nemaline myopathy patients

    PMID:11738357

    Open questions at the time
    • Effect on actin binding was predicted, not directly assayed
    • No biophysical measurement of the contractile defect
  2. 2007 Medium

    Showed that an in-frame deletion disrupting the coiled-coil heptad repeat incorporates into sarcomeres and likely acts dominant-negatively, linking structural disruption to cap disease.

    Evidence Genetic sequencing and 2D-gel electrophoresis of patient muscle

    PMID:17434307 PMID:19345583

    Open questions at the time
    • Dominant-negative mechanism inferred rather than directly demonstrated
    • No reconstituted thin-filament functional readout
  3. 2012 High

    Provided the first direct biochemical demonstration that disease mutations alter actin affinity, Ca2+ activation, and protein conformation, moving from genetic association to assayed mechanism.

    Evidence In vitro actin co-sedimentation, Ca2+-activation of contractility, and conformation analysis of four mutations

    PMID:22084935

    Open questions at the time
    • Did not resolve tropomyosin position on the filament
    • Cross-bridge cycle kinetics not measured
  4. 2013 High

    Connected reduced actin affinity to defective sarcomeric incorporation, nemaline rod formation, and altered force/Ca2+ sensitivity in patient fibres, and corroborated the polymerization defect in vivo.

    Evidence Recombinant binding assay, C2C12 transfection, single patient myofibre force measurement, and zebrafish overexpression

    PMID:23378224 PMID:23413262

    Open questions at the time
    • Mechanism limited to one mutation (K7del)
    • Head-to-tail polymerization defect inferred from localization
  5. 2014 Medium

    Correlated molecular phenotype with clinical presentation across many families, establishing that increased Ca2+ sensitivity (hypercontractility) tracks with joint contractures.

    Evidence Genotype-phenotype analysis of TPM2-mutation families with in silico structural prediction

    PMID:24692096

    Open questions at the time
    • Many variant effects predicted in silico, not measured
    • Ca2+ sensitivity data drawn from prior studies
  6. 2017 Medium

    Defined at the structural level how individual mutations reposition tropomyosin on actin and shift the blocked/closed/open equilibrium to produce hyper- or hypocontractile states.

    Evidence Polarized fluorescence microscopy of reconstituted ghost fibres during the ATPase cycle (Q147P, Glu139del, Arg91Gly)

    PMID:26708479 PMID:29097206 PMID:29196649

    Open questions at the time
    • Each result from a single lab and method
    • Quantitative myosin kinetics not directly measured
  7. 2019 Medium

    Extended the positional model to additional weakness-causing mutations and compared heterodimer versus homodimer behavior, linking blocked-position freezing to low Ca2+ sensitivity.

    Evidence Polarized fluorescence microscopy of reconstituted ghost fibres (E41K, R133W; αβ and ββ dimers)

    PMID:29792862 PMID:31864708

    Open questions at the time
    • Single-lab reconstitution data
    • In vivo relevance of homo- vs heterodimer differences unresolved
  8. 2021 High

    Systematically partitioned mutations into hyper- and hypocontractile classes using direct ATPase and Ca2+ sensitivity measurements, consolidating the two-class mechanistic model.

    Evidence Actin co-sedimentation, actomyosin ATPase, Ca2+ sensitivity, and trypsin-susceptibility assays (Q93H, E97K)

    PMID:33919826

    Open questions at the time
    • Two mutations only
    • Did not address filament turnover or thin-filament assembly
  9. 2024 High

    Resolved the mechanochemical basis of the two phenotype classes, showing hypercontractile mutations accelerate and hypocontractile mutations decelerate myosin product release.

    Evidence FRET orientation assays, myosin ATPase, in vitro motility, and single-turnover kinetics (D20H, E181K, E41K, N202K)

    PMID:38156416

    Open questions at the time
    • Performed without full troponin regulation in some readouts
    • Structural cause of orientation changes not solved
  10. 2025 High

    Dissected troponin-dependent versus troponin-independent regulation and mapped N-terminal mutations to enhanced tropomyosin-troponin affinity, refining how variants distort Ca2+-regulated switching.

    Evidence Actomyosin ATPase, in vitro motility, Tpm-troponin binding, and Arrhenius analysis of four variants

    PMID:40657867

    Open questions at the time
    • Mechanism of N-terminal affinity enhancement unresolved
    • Effects measured in reconstituted not cellular systems
  11. 2025 High

    Established a non-muscle role for cytoplasmic Tpm2 isoforms as direct inhibitors of fascin-1-mediated actin bundling, distinguishing isoform-specific cytoskeletal regulation.

    Evidence Pull-down, co-sedimentation, bundling assays, and confocal microscopy in SAOS-2 cells

    PMID:40887664

    Open questions at the time
    • Cellular consequences for migration/metastasis not directly tested
    • Structural basis of Tpm2-fascin competition unknown
  12. 2023 Medium

    Defined a tumor-suppressive signaling mechanism in which TPM2 competes with YAP1 for PDLIM7 to retain YAP1 in the cytoplasm in its phosphorylated, inactive state.

    Evidence Reciprocal Co-IP, PDZ-motif deletion mapping, immunofluorescence, and xenograft assays

    PMID:36823643

    Open questions at the time
    • Single-lab finding
    • Link between cytoskeletal and signaling functions not integrated
  13. 2025 Medium

    Implicated TPM2 in regulating cell migration, invasion, apoptosis, and NF-κB-driven inflammation, indicating broad non-sarcomeric functions tied to actomyosin and signaling.

    Evidence Knockdown/overexpression with migration, apoptosis, ROCK-inhibitor, and cytokine/NF-κB readouts in epithelial, neuroepithelial, and trophoblast cells

    PMID:27333992 PMID:28378936 PMID:29221121 PMID:41297249

    Open questions at the time
    • Mechanistic links established mostly by association
    • No domain mapping or rescue for several effects

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the distinct sarcomeric, cytoskeletal-bundling, and signaling functions of TPM2 isoforms are integrated, and whether a unified structural framework explains both contractile and non-muscle roles, remains unresolved.
  • No structural model linking position changes to non-muscle isoform function
  • Isoform-specific in vivo functions not delineated
  • Cross-talk between actin-bundling and YAP/NF-κB signaling untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008092 cytoskeletal protein binding 5 GO:0098772 molecular function regulator activity 4 GO:0005198 structural molecule activity 3
Localization
GO:0005856 cytoskeleton 3 GO:0005829 cytosol 2
Pathway
R-HSA-1643685 Disease 4 R-HSA-397014 Muscle contraction 4 R-HSA-162582 Signal Transduction 2
Partners
ACTA1COFILIN-2 (CFL2)FASCIN-1 (FSCN1)PDLIM7TNNTYAP1
Complex memberships
thin filament (actin-tropomyosin-troponin)

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Two heterozygous missense mutations in TPM2 (beta-tropomyosin) affect conserved amino acids and are expressed at the mutant allele level; the mutations are predicted to affect tropomyosin dimer formation and actin-binding properties, establishing TPM2 mutations as a cause of nemaline myopathy. SSCP analysis, sequencing, expression analysis of mutant allele Neuromuscular disorders : NMD Medium 11738357
2007 An in-frame deletion of Glu139 (p.Glu139del) in TPM2 disrupts the seven-amino acid repeat essential for the coiled-coil structure, impairing tropomyosin-actin interaction and causing cap disease; 2D-gel electrophoresis confirmed mutant protein incorporates into sarcomeric structures where it likely exerts a dominant-negative effect. Genetic sequencing, 2D-gel electrophoresis of patient muscle Neuromuscular disorders : NMD Medium 17434307 19345583
2012 Four disease-causing TPM2 mutations (in nemaline myopathy and cap myopathy) cause altered affinity of beta-tropomyosin for actin as measured by in vitro binding assays; two mutations also cause defective Ca2+ activation of contractility; two mutations cause altered protein conformation mapped to actin-binding regions. In vitro actin co-sedimentation assay, Ca2+-activation of contractility assay, conformation analysis The Biochemical journal High 22084935
2013 The TPM2 p.K7del mutation reduces beta-tropomyosin affinity for actin, impairs incorporation into sarcomeres in C2C12 myotubes (mutant accumulates in nemaline rods), disrupts head-to-tail polymerization, and increases myofilament calcium sensitivity as measured by force in single dissected patient myofibres. Recombinant protein actin-binding assay, C2C12 myotube transfection, 2D-gel electrophoresis of patient muscle, single myofibre force measurements Brain : a journal of neurology High 23378224
2013 Expression of p.K7del beta-tropomyosin in zebrafish disrupts thin filament localization and alters sarcomere length in vivo, consistent with impaired head-to-tail polymerization of TPM2 dimers. Zebrafish in vivo overexpression, fluorescence microscopy of sarcomere structure Brain : a journal of neurology Medium 23413262
2014 Genotype-phenotype analysis of 53 TPM2-mutation families reveals that five TPM2 mutations cause increased Ca2+ sensitivity (hypercontractile molecular phenotype), correlated with joint contractures, while non-hypercontractile mutations correlate with axial contractures; in silico analysis indicates most mutations affect tropomyosin-actin association or head-to-tail binding. Ca2+ sensitivity measurements (from prior studies referenced), clinical correlation across 93 families, in silico structural prediction Human mutation Medium 24692096
2015 The myopathy-causing Q147P mutation in beta-tropomyosin (TPM2) shifts tropomyosin strands closer to the center of the actin filament (open position) despite reduced actin affinity, increases the proportion of strong-binding myosin cross-bridges during ATPase cycle, and disrupts cooperation of actin and myosin heads. Polarized fluorimetry in reconstituted ghost muscle fibres, co-sedimentation assay for actin affinity Biochimica et biophysica acta Medium 26708479
2016 Epigenetic silencing of TPM2 via promoter DNA methylation suppresses its expression in colorectal cancer; treatment with demethylation agent 5-AZA restores TPM2 expression; reconstitution of TPM2 suppresses cell proliferation and migration; loss of TPM2 is associated with RhoA activation. Promoter methylation analysis, 5-AZA demethylation assay, TPM2 overexpression/knockdown in cancer cell lines, proliferation/migration assays, RhoA activity measurement Tumour biology Medium 27333992
2017 The Glu139del mutation in TPM2 does not alter tropomyosin affinity for actin but markedly increases tropomyosin flexibility, keeps tropomyosin strands near the inner domain of actin (blocked-position movement inhibited at low Ca2+), increases troponin-mediated switching on/off of actin monomers, and decreases strong myosin head binding at high Ca2+ while increasing it at relaxation—mechanistically explaining hypercontractile Ca2+ sensitivity and muscle weakness. Polarized fluorescence microscopy of reconstituted ghost fibres, actin affinity assay Scientific reports Medium 29196649
2017 Knockdown of Tpm2.1 in MCF10A breast epithelial cells retards collective cell migration but increases single cell migration and invasion; this is associated with enhanced actomyosin contractility, increased E-cadherin/β-catenin expression, decreased AXL receptor tyrosine kinase, and is rescued by ROCK inhibition. siRNA/shRNA knockdown, wound healing and transwell migration/invasion assays, Western blotting, ROCK inhibitor treatment, spheroid re-plating assay Oncotarget Medium 29221121
2017 Overexpression of Tpm2.1 in rat neuroepithelial cells enhances sensitivity to anoikis and to jasplakinolide-induced apoptosis; this is accompanied by enhanced mitochondrial depolarization and elevated levels of Bak, Mcl-1, Bcl-2, and phospho-p53 (Ser392); jasplakinolide treatment of Tpm2.1-overexpressing cells reduces Mcl-1, Bcl-2, and p53(Ser392). Tpm2.1 overexpression in rat cells, apoptosis assays (anoikis, jasplakinolide), mitochondrial membrane potential assay, Western blotting of apoptosis regulators Cytoskeleton (Hoboken, N.J.) Medium 28378936
2017 The Arg91Gly mutation in TPM2 markedly decreases bending stiffness of beta-tropomyosin in thin filaments; during ATPase cycle, mutant tropomyosin remains near the open position allowing strong myosin head binding to actin even at low Ca2+, mechanistically explaining high Ca2+ sensitivity and contractures associated with this distal arthrogryposis mutation. Polarized fluorescence microscopy of reconstituted ghost fibres during ATPase cycle Biochemical and biophysical research communications Medium 29097206
2017 Smad4 SUMOylation (by E3 ligase PIAS1 at Lys-113 and Lys-159 in hippocampus) drives TPM2 upregulation; knockdown of TPM2 in rats impairs spatial learning and memory; TPM2 mRNA and protein increase after spatial training; the myopathy-associated TPM2-E122K mutation reduces TPM2 expression and impairs spatial memory in rats. SUMO site mutagenesis, rat hippocampal injection/knockdown, behavioral memory tests, Western blot, mRNA quantification BMC biology Medium 29183317
2018 The Glu41Lys (E41K) mutation in TPM2 inhibits troponin's ability to shift tropomyosin to the closed position at high Ca2+, restraining thin filament transition from 'off' to 'on' state; it also inhibits S1-driven shift to the open position and inhibits switching off of actin monomers at low Ca2+—explaining reduced Ca2+ sensitivity and muscle weakness in nemaline myopathy/cap disease. Polarized fluorescence microscopy of reconstituted ghost fibres during ATPase cycle Biochemical and biophysical research communications Medium 29792862
2019 The R133W mutation in Tpm2.2 decreases the amount of strongly actin-bound myosin heads and number of switched-on actin monomers at high Ca2+, inhibits tropomyosin shifting towards the open position, and freezes mutant tropomyosin near the blocked position; at low Ca2+, fewer strongly-bound myosin heads contribute to low myofilament Ca2+-sensitivity—explaining muscle weakness in Sheldon-Hall syndrome. Polarized fluorescence microscopy of reconstituted ghost fibres (αβ-Tpm heterodimers and ββ-Tpm homodimers) during ATPase cycle Biochemical and biophysical research communications Medium 31864708
2021 Mutations Q93H and E97K in Tpm2.2 both decrease actin affinity of homo- and heterodimers in vitro; Q93H strongly decreases actomyosin ATPase activation and reduces Ca2+ sensitivity (hypocontractile); E97K causes hyperactivation of ATPase and increased Ca2+ sensitivity (hypercontractile); both mutations alter tropomyosin dynamics on the filament. In vitro actin co-sedimentation, actomyosin ATPase assay, Ca2+ sensitivity measurements, trypsin susceptibility assay for dynamics International journal of molecular sciences High 33919826
2022 Expression of dominant pathogenic TPM2 variants in Drosophila embryos significantly affected muscle development and function; transient overexpression disrupted mouse myotube morphogenesis in vitro and zebrafish muscle development in vivo, establishing disrupted myogenesis as a pathomechanism of TPM2 disorders. Drosophila muscle development assays, mouse myotube morphogenesis assay, zebrafish in vivo overexpression JCI insight Medium 35579956
2023 TPM2 competes with YAP1 for binding to PDLIM7 via its PDZ-binding motif; this competition prevents PDLIM7-mediated nuclear translocation of YAP1, sequestering YAP1 in the cytoplasm where it is phosphorylated at S127 and inactivated/degraded, thereby suppressing YAP1 target gene expression and prostate cancer progression. Co-immunoprecipitation, immunofluorescence localization, Western blotting (p-YAP1-S127), PDZ-binding motif deletion mutant, in vitro cell proliferation/invasion assays, xenograft tumor assay Cell & bioscience Medium 36823643
2024 Hypercontractile mutations D20H and E181K in Tpm2.2 alter the binding geometry and orientation of tropomyosin on actin (by FRET), stimulate myosin motor performance and accelerate product (ADP/Pi) release kinetics; hypocontractile mutations E41K and N202K inhibit actin activation of myosin ATPase, motor activity, and decelerate product release—demonstrating opposite mechanochemical effects on the cross-bridge cycle. FRET assays for Tpm orientation on actin, myosin ATPase assay, in vitro motility assay, single ATP turnover kinetics FASEB journal High 38156416
2025 At low Ca2+, all four pathogenic Tpm2.2 variants (D20H, E181K, E41K, N202K) inhibit troponin-regulated actomyosin ATPase without affecting troponin binding to actin; at activating Ca2+, hypocontractile mutants suppress ATPase and motor function while hypercontractile mutants enhance myosin-driven actin translocation; N-terminal mutations (D20H, E181K) enhance high-affinity Tpm2.2-troponin interactions; hypercontractile mutants increase Ca2+ sensitivity while hypocontractile mutants decrease it. In vitro actomyosin ATPase assay, in vitro motility assay, Tpm-troponin binding assay, Arrhenius analysis of temperature dependence The FEBS journal High 40657867
2025 Cytoplasmic TPM2 isoforms (Tpm2.1, Tpm2.3, Tpm2.4) directly interact with fascin-1 (pull-down assay) and inhibit fascin-1-mediated actin bundling by reducing fascin-1 affinity for actin; Tpm2 occupancy on actin filaments partially displaces fascin-1; fascin-1 binding does not affect Tpm2 affinity for actin; Tpm2.4 shows highest actin and fascin-1 affinities; overexpression of Tpm2 isoforms in SAOS-2 LM5 cells reduces fascin co-localization with actin. High-speed centrifugation (actin affinity), low-speed centrifugation and fluorescence microscopy (bundling), pull-down assay (direct Tpm2-fascin interaction), confocal microscopy in SAOS-2 cells Biological research High 40887664
2025 TPM2 overexpression in HTR-8/SVneo trophoblast cells enhances migration and invasion, suppresses IL-6, IL-1β, and IL-8 production, inhibits IκBα degradation, and blocks nuclear translocation of NF-κB p65, establishing TPM2 as a suppressor of NF-κB-mediated inflammation. TPM2 overexpression in trophoblast cells, migration/invasion assays, cytokine ELISA, Western blot for IκBα and p65 nuclear translocation Tissue & cell Medium 41297249
2026 Wild-type Tpm2.2 inhibits spontaneous actin polymerization; hypercontractile D20H and E181K further decrease polymerization rate; hypocontractile E41K and N202K stabilize filaments under actomyosin-driven conditions increasing filament length (abolished by troponin); all variants slightly decrease cofilin-2 affinity for F-actin; Tpm2.2-N202K inhibits cofilin-2-dependent depolymerization while E181K increases susceptibility; the Tpm2.2-troponin complex protects filaments from cofilin-2-induced disassembly. In vitro actin polymerization assay, filament stability and length measurement under actomyosin conditions, cofilin-2 binding and depolymerization assays, structural modeling bioRxivpreprint Medium 42239403

Source papers

Stage 0 corpus · 49 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Mutations in the beta-tropomyosin (TPM2) gene--a rare cause of nemaline myopathy. Neuromuscular disorders : NMD 188 11738357
1995 Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions. The Journal of cell biology 125 7844152
2014 Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies. Human mutation 92 24692096
2007 Cap disease caused by heterozygous deletion of the beta-tropomyosin gene TPM2. Neuromuscular disorders : NMD 81 17434307
2007 Congenital myopathy with nemaline rods and cap structures caused by a mutation in the beta-tropomyosin gene (TPM2). Archives of neurology 71 17846275
2019 TPM2 as a potential predictive biomarker for atherosclerosis. Aging 53 31487691
2013 K7del is a common TPM2 gene mutation associated with nemaline myopathy and raised myofibre calcium sensitivity. Brain : a journal of neurology 48 23378224
2012 Abnormal actin binding of aberrant β-tropomyosins is a molecular cause of muscle weakness in TPM2-related nemaline and cap myopathy. The Biochemical journal 45 22084935
2013 Novel deletion of lysine 7 expands the clinical, histopathological and genetic spectrum of TPM2-related myopathies. Brain : a journal of neurology 43 23413262
2008 New morphologic and genetic findings in cap disease associated with beta-tropomyosin (TPM2) mutations. Neurology 39 19047562
2012 Whole-Body muscle MRI in a series of patients with congenital myopathy related to TPM2 gene mutations. Neuromuscular disorders : NMD 37 22980765
2009 Cap disease due to mutation of the beta-tropomyosin gene (TPM2). Neuromuscular disorders : NMD 37 19345583
2016 Epigenetic silencing of TPM2 contributes to colorectal cancer progression upon RhoA activation. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 30 27333992
2009 Skeletal muscle contractile gene (TNNT3, MYH3, TPM2) mutations not found in vertical talus or clubfoot. Clinical orthopaedics and related research 30 19142688
2017 Tropomyosin isoform Tpm2.1 regulates collective and amoeboid cell migration and cell aggregation in breast epithelial cells. Oncotarget 26 29221121
2016 Functional Assessment of Clubfoot Associated HOXA9, TPM1, and TPM2 Variants Suggests a Potential Gene Regulation Mechanism. Clinical orthopaedics and related research 22 27020427
2016 iTRAQ-based quantitative analysis of cancer-derived secretory proteome reveals TPM2 as a potential diagnostic biomarker of colorectal cancer. Frontiers of medicine 21 27283175
2017 Tumor suppressor tropomyosin Tpm2.1 regulates sensitivity to apoptosis beyond anoikis characterized by changes in the levels of intrinsic apoptosis proteins. Cytoskeleton (Hoboken, N.J.) 20 28378936
2023 TPM2 attenuates progression of prostate cancer by blocking PDLIM7-mediated nuclear translocation of YAP1. Cell & bioscience 19 36823643
2012 Mutations in TPM2 and congenital fibre type disproportion. Neuromuscular disorders : NMD 16 22832343
2018 Novel mutations in TPM2 and PIEZO2 are responsible for distal arthrogryposis (DA) 2B and mild DA in two Chinese families. BMC medical genetics 14 30285720
2015 Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycle. Biochimica et biophysica acta 14 26708479
2017 Molecular mechanisms of dysfunction of muscle fibres associated with Glu139 deletion in TPM2 gene. Scientific reports 13 29196649
2014 Frequency and phenotype of patients carrying TPM2 and TPM3 gene mutations in a cohort of 94 patients with congenital myopathy. Neuromuscular disorders : NMD 13 24507666
2017 Smad4 SUMOylation is essential for memory formation through upregulation of the skeletal myopathy gene TPM2. BMC biology 12 29183317
2010 A novel splice variant of the beta-tropomyosin (TPM2) gene in prostate cancer. Molecular carcinogenesis 12 20336778
2022 A pathogenic mechanism associated with myopathies and structural birth defects involves TPM2-directed myogenesis. JCI insight 11 35579956
2021 Mutations Q93H and E97K in TPM2 Disrupt Ca-Dependent Regulation of Actin Filaments. International journal of molecular sciences 11 33919826
2019 The molecular mechanism of muscle dysfunction associated with the R133W mutation in Tpm2.2. Biochemical and biophysical research communications 11 31864708
2016 A novel TPM2 gene splice-site mutation causes severe congenital myopathy with arthrogryposis and dysmorphic features. Journal of applied genetics 11 27726070
2017 The reason for a high Ca2+-sensitivity associated with Arg91Gly substitution in TPM2 gene is the abnormal behavior and high flexibility of tropomyosin during the ATPase cycle. Biochemical and biophysical research communications 9 29097206
1995 Assignment of the human beta tropomyosin gene (TPM2) to band 9p13 by fluorescence in situ hybridisation. Cytogenetics and cell genetics 8 7606936
2020 A recurrent pathogenic variant in TPM2 reveals further phenotypic and genetic heterogeneity in multiple pterygium syndrome-related disorders. Clinical genetics 7 32092148
2013 First Korean family with a mutation in TPM2 associated with Sheldon-Hall syndrome. Journal of Korean medical science 6 23678273
2024 Relevance Analysis of TPM2 and Clinicopathological Characteristics in Breast Cancer. International journal of general medicine 5 38221941
2023 In silico whole-transcriptome analysis reveals a potential hsa_circ_0000375-miR-424-5p-TPM2/SRPX/SRGAP1 regulatory network related to liver metastasis of colorectal cancer. Heliyon 5 37954397
2022 A Potential Target for Clinical Atherosclerosis: A Novel Insight Derived from TPM2. Aging and disease 5 35371599
2020 Demonstration of beta-tropomyosin (Tpm2) and duplication of the alpha-slow tropomyosin gene (TPM3) in Atlantic salmon Salmo salar. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology 4 32283206
2020 Homozygous intronic variants in TPM2 cause recessively inherited Escobar variant of multiple pterygium syndrome and congenital myopathy. Neuromuscular disorders : NMD 4 33558124
2019 Establishment of a human induced pluripotent stem cell line (SDQLCHi004-A) from a patient with nemaline myopathy-4 disease carrying heterozygous mutation in TPM2 gene. Stem cell research 4 31526942
2018 The reason for the low Ca2+-sensitivity of thin filaments associated with the Glu41Lys mutation in the TPM2 gene is "freezing" of tropomyosin near the outer domain of actin and inhibition of actin monomer switching off during the ATPase cycle. Biochemical and biophysical research communications 4 29792862
2025 Myopathy-linked mutations in TPM2 and their impact on troponin-mediated regulation of actomyosin contractility. The FEBS journal 2 40657867
2025 Tropomyosin isoforms encoded by TPM2 control the actin-bundling activity of fascin-1. Biological research 2 40887664
2024 Mechanochemical consequences of myopathy-linked mutations in Tpm2.2 on striated muscle contractility. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2 38156416
2021 Abnormal TPM2 expression is involved in regulation of atherosclerosis progression via mediating RhoA signaling in vitro. Archives of medical science : AMS 2 39439675
2025 TPM2 regulates contractility and biomechanical properties in trabecular meshwork cells. Scientific reports 1 41266745
2026 Disease-associated mutations in TPM2 alter regulation of actin filament stability and cofilin-dependent dynamics. bioRxiv : the preprint server for biology 0 42239403
2025 TPM2 as a novel inflammatory regulator in severe obstetric disorders: Integrative bioinformatics and functional validation. Tissue & cell 0 41297249
2024 A TPM2 mutation causes congenital myopathy with fibre-type disproportion. Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology 0 39477909

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