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    Tpm1 tropomyosin 1, alpha [ Mus musculus (house mouse) ]

    Gene ID: 22003, updated on 21-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    TPM1 mediates inflammation downstream of TREM2 via the PKA/CREB signaling pathway.

    TPM1 mediates inflammation downstream of TREM2 via the PKA/CREB signaling pathway.
    Li R, Zhang J, Wang Q, Cheng M, Lin B., Free PMC Article

    10/22/2022
    Genetic resiliency associated with dominant lethal TPM1 mutation causing atrial septal defect with high heritability.

    Genetic resiliency associated with dominant lethal TPM1 mutation causing atrial septal defect with high heritability.
    Teekakirikul P, Zhu W, Xu X, Young CB, Tan T, Smith AM, Wang C, Peterson KA, Gabriel GC, Ho S, Sheng Y, Moreau de Bellaing A, Sonnenberg DA, Lin JH, Fotiou E, Tenin G, Wang MX, Wu YL, Feinstein T, Devine W, Gou H, Bais AS, Glennon BJ, Zahid M, Wong TC, Ahmad F, Rynkiewicz MJ, Lehman WJ, Keavney B, Alastalo TP, Freckmann ML, Orwig K, Murray S, Ware SM, Zhao H, Feingold B, Lo CW., Free PMC Article

    05/7/2022
    Accumulation of systematic TPM1 mediates inflammation and neuronal remodeling by phosphorylating PKA and regulating the FABP5/NF-kappaB signaling pathway in the retina of aged mice.

    Accumulation of systematic TPM1 mediates inflammation and neuronal remodeling by phosphorylating PKA and regulating the FABP5/NF-κB signaling pathway in the retina of aged mice.
    Li R, Liang Y, Lin B., Free PMC Article

    05/7/2022
    The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect.

    The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect.
    Hornos F, Feng HZ, Rizzuti B, Palomino-Schätzlein M, Wieczorek D, Neira JL, Jin JP., Free PMC Article

    08/28/2021
    Tropomyosin pseudo-phosphorylation results in dilated cardiomyopathy.

    Tropomyosin pseudo-phosphorylation results in dilated cardiomyopathy.
    Rajan S, Jagatheesan G, Petrashevskaya N, Biesiadecki BJ, Warren CM, Riddle T, Liggett S, Wolska BM, Solaro RJ, Wieczorek DF., Free PMC Article

    05/25/2019
    Stress fibre formation and up-regulation of alpha-smooth muscle actin (alphaSMA) induced by TGFbeta2 could be reversed by Tpm1/2 knock-down by siRNA.

    FGF2 antagonizes aberrant TGFβ regulation of tropomyosin: role for posterior capsule opacity.
    Kubo E, Shibata S, Shibata T, Kiyokawa E, Sasaki H, Singh DP., Free PMC Article

    10/14/2017
    The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin position.

    The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position.
    Mun JY, Kensler RW, Harris SP, Craig R., Free PMC Article

    11/12/2016
    three-dimensional structure of F-actin at a resolution of 3.7 A in complex with tropomyosin at a resolution of 6.5 A, determined by electron cryomicroscopy

    Structure of the F-actin-tropomyosin complex.
    von der Ecken J, Müller M, Lehman W, Manstein DJ, Penczek PA, Raunser S., Free PMC Article

    03/28/2015
    data also identify a novel alphaTM1/Tmod1-based pathway stabilizing F-actin at cell-cell junctions, which may be required for maintenance of cell shapes during embryonic cardiac morphogenesis.

    Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo.
    McKeown CR, Nowak RB, Gokhin DS, Fowler VM., Free PMC Article

    01/3/2015
    This is the first study to demonstrate that decreasing phosphorylation of tropomyosin can rescue a hypertrophic cardiomyopathic phenotype.

    Decreasing tropomyosin phosphorylation rescues tropomyosin-induced familial hypertrophic cardiomyopathy.
    Schulz EM, Wilder T, Chowdhury SA, Sheikh HN, Wolska BM, Solaro RJ, Wieczorek DF., Free PMC Article

    12/7/2013
    the link between flexibility of TM and its function in ejecting hearts.

    Conserved Asp-137 is important for both structure and regulatory functions of cardiac α-tropomyosin (α-TM) in a novel transgenic mouse model expressing α-TM-D137L.
    Yar S, Chowdhury SAK, Davis RT 3rd, Kobayashi M, Monasky MM, Rajan S, Wolska BM, Gaponenko V, Kobayashi T, Wieczorek DF, Solaro RJ., Free PMC Article

    08/31/2013
    Tm pseudo-phosphorylation slows deactivation of the thin filament and muscle force relaxation dynamics in the absence of dynamic and steady-state effects on muscle activation.

    Tropomyosin Ser-283 pseudo-phosphorylation slows myofibril relaxation.
    Nixon BR, Liu B, Scellini B, Tesi C, Piroddi N, Ogut O, Solaro RJ, Ziolo MT, Janssen PM, Davis JP, Poggesi C, Biesiadecki BJ., Free PMC Article

    06/22/2013
    Tropomyosin dephosphorylation results in myocyte hypertrophy with increases in SERCA2a expression.

    Tropomyosin dephosphorylation results in compensated cardiac hypertrophy.
    Schulz EM, Correll RN, Sheikh HN, Lofrano-Alves MS, Engel PL, Newman G, Schultz Jel J, Molkentin JD, Wolska BM, Solaro RJ, Wieczorek DF., Free PMC Article

    03/30/2013
    The results identify a novel mode of myofilament desensitization to Ca(2+) associated with a DCM linked switch in TPM1-kappa.

    Expression of tropomyosin-κ induces dilated cardiomyopathy and depresses cardiac myofilament tension by mechanisms involving cross-bridge dependent activation and altered tropomyosin phosphorylation.
    Karam CN, Warren CM, Rajan S, de Tombe PP, Wieczorek DF, Solaro RJ., Free PMC Article

    10/1/2011
    Developed mouse model of familial hypertrophic cardiomyopathy with a mutation in the thin filament protein alpha-tropomyosin.

    Rescue of tropomyosin-induced familial hypertrophic cardiomyopathy mice by transgenesis.
    Jagatheesan G, Rajan S, Petrashevskaya N, Schwartz A, Boivin G, Arteaga GM, Solaro RJ, Liggett SB, Wieczorek DF.

    01/21/2010
    Two transgenic lines of mutated alpha-TM demonstrated alterations in myocardial contractility differently.

    Charged residue alterations in the inner-core domain and carboxy-terminus of alpha-tropomyosin differentially affect mouse cardiac muscle contractility.
    Gaffin RD, Tong CW, Zawieja DC, Hewett TE, Klevitsky R, Robbins J, Muthuchamy M., Free PMC Article

    01/21/2010
    the N terminus is a critical determinant of TM1 functions, which in turn determines the organization of stress fibers.

    N terminus is essential for tropomyosin functions: N-terminal modification disrupts stress fiber organization and abolishes anti-oncogenic effects of tropomyosin-1.
    Bharadwaj S, Hitchcock-DeGregori S, Thorburn A, Prasad GL.

    01/21/2010
    A point mutation in alpha-TM causes a disease similar to familial hypertophic cardiomyopahy.

    A mouse model of familial hypertrophic cardiomyopathy caused by a alpha-tropomyosin mutation.
    Prabhakar R, Petrashevskaya N, Schwartz A, Aronow B, Boivin GP, Molkentin JD, Wieczorek DF.

    01/21/2010
    PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing.

    The PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing.
    Gromak N, Rideau A, Southby J, Scadden AD, Gooding C, Hüttelmaier S, Singer RH, Smith CW., Free PMC Article

    01/21/2010
    charge changes at the carboxy-terminal of alpha-TM alter the functional characteristics of the heart at both the whole organ and myofilament levels.

    Charged residue changes in the carboxy-terminus of alpha-tropomyosin alter mouse cardiac muscle contractility.
    Gaffin RD, Gokulan K, Sacchettini JC, Hewett T, Klevitsky R, Robbins J, Muthuchamy M., Free PMC Article

    01/21/2010
    signaling by alpha-tropomyosin may have a role in familial hypertrophic cardiomyopathy

    Altered signaling surrounding the C-lobe of cardiac troponin C in myofilaments containing an alpha-tropomyosin mutation linked to familial hypertrophic cardiomyopathy.
    Burkart EM, Arteaga GM, Sumandea MP, Prabhakar R, Wieczorek DF, Solaro RJ.

    01/21/2010
    Chronic activation of p38alpha MAPK directly depresses sarcomeric function in association with decreased phosphorylation of alpha-tropomyosin.

    p38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity.
    Vahebi S, Ota A, Li M, Warren CM, de Tombe PP, Wang Y, Solaro RJ.

    01/21/2010
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