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The tendency of smooth muscle tropomyosin to form semi-rigid polymers with continuous and undampened rigidity may compensate for the lack of troponin-based structural support in smooth muscles.
Deletion of regions 2-3 in tropomyosin (show TPM2 Proteins) alpha resulted in an 60 % decrease in both isometric tension and stiffness of tropomyosin (show TPM2 Proteins)-reconstituted myocardium.
Tropomyosin (show TPM2 Proteins) is primarily responsible for the change in the kinetic constants of the elementary steps of the cross bridge cycle.
Tm affects the conformation of actin so as to increase the area of hydrophobic interaction between actin and myosin molecules
Stress fibre formation and up-regulation of alpha-smooth muscle actin (show ACTG2 Proteins) (alphaSMA (show ACTA2 Proteins)) induced by TGFbeta2 could be reversed by Tpm1/2 knock-down by siRNA.
The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin (show TPM2 Proteins) position.
three-dimensional structure of F-actin at a resolution of 3.7 A in complex with tropomyosin (show TPM2 Proteins) at a resolution of 6.5 A, determined by electron cryomicroscopy
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.
This is the first study to demonstrate that decreasing phosphorylation of tropomyosin (show TPM2 Proteins) can rescue a hypertrophic cardiomyopathic phenotype.
Tropomyosin (show TPM2 Proteins) dephosphorylation results in myocyte hypertrophy with increases in SERCA2a (show ATP2A2 Proteins) expression.
The results identify a novel mode of myofilament desensitization to Ca(2 (show CA2 Proteins)+) associated with a DCM linked switch in TPM1-kappa.
signaling by alpha-tropomyosin may have a role in familial hypertrophic cardiomyopathy
A point mutation in alpha-TM causes a disease similar to familial hypertophic cardiomyopahy.
PTB (show PTBP1 Proteins) interacting protein raver1 (show RAVER1 Proteins) regulates alpha-tropomyosin alternative splicing.
Missense variant (p.Leu113Val) in TPM1 causes left ventricular non-compaction with Ebstein anomaly in five members of the family.
miR (show MLXIP Proteins)-107 overexpression promoted U2OS cell viability, migration, and invasion via downregulation of TPM1 and might be through activating the MEK (show MAP2K1 Proteins)/ERK (show EPHB2 Proteins) and NF-kappaB (show NFKB1 Proteins) signaling pathways.
Functional effects of substitutions I92T and V95A in actin-binding period 3 of tropomyosin (show TPM2 Proteins).
This study demonstrated that sarcomeric TPM1 plays vital roles in cardiogenesis and is a suitable candidate gene for screening individuals with isolated congenital heart defects .
Tpm (show TPMT Proteins) isoforms 1.8/9 are enriched in the lamellipodium of fibroblasts as detected with a novel isoform-specific monoclonal antibody. RNAi-mediated silencing of Tpm1.8/9 led to an increase of Arp2 (show ACTR2 Proteins)/3 accumulation at the cell periphery and a decrease in the persistence of lamellipodia and cell motility.
TPM1-AS regulates the alternative splicing of TPM1 through an interaction with RBM4 (show RBM4 Proteins) and involves in TPM1-mediated filopodium formation and migration of cancer cells
The impact of tropomyosins on actin filament assembly is isoform specific.
TPM1 is the second gene linked to EA with LVNC in humans, implicating overlap in the molecular basis of structural and myopathic heart disease.
data demonstrate that the K15N mutation alters pointed end dynamics by affecting molecular interactions between Tpm1.1, Lmod2 (show LMOD2 Proteins) and Tmod1 (show TMOD1 Proteins).
We show that the phosphorylation of cTnI and alphaTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not.
The results indicate that cross-linking significantly affects properties of Tpm (show TPMT Proteins) and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm (show TPMT Proteins) in human heart diseases.
altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
analysis of the thin filament associated with the R167H and K168E substitutions in tropomyosin (show TPM2 Proteins) Tpm1.1
We propose that TR100 acts to compromise the integrity of Tpm cables rather than prevent overlap complex formation. Our data suggests that TR100 is incorporated into the growing actin-Tpm co-polymer given that its effects cannot be observed on pre-formed Tpm3.1/actin filaments
Maximal Ca(2 (show CA2 Proteins)+) activated force was the same in alphaalphaTm versus betabetaTm myofibrils, but betabetaTm myofibrils showed a marked slowing of relaxation and an impairment of regulation under resting conditions
Tmod1 (show TMOD1 Proteins) and Tmod3 (show TMOD3 Proteins) showed somewhat different tropomyosin (show TPM2 Proteins)-binding site utilization.
Thermal denaturation of rabbit cardiac alpha,alpha-tropomyosin is monitored at neutral pH and compared to shark tropomyosin (show TPM2 Proteins), showing that amino acid substitutions predicted to be unfavorable in one temperature regime are desirable in another.
The rotational motion of a spin label covalently bound to the side chain of a cysteine genetically incorporated into rabbit skeletal muscle tropomyosin (show TPM2 Proteins), was measured.
a computational search assessing electrostatic interactions for multiple azimuthal locations, z-positions, and pseudo-rotations of tropomyosin on F-actin was performed.
This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy.
, alpha-tropomyosin 2
, alpha-tropomyosin of skeletal fast muscle
, tropomyosin (CTm4)
, tropomyosin (CTm7)
, tropomyosin alpha-1 chain
, tropomyosin 1 alpha chain
, alpha tropomyosin
, hepatoma alpha tropomyosin
, smooth muscle alpha-tropomyosin
, striated muscle alpha-tropomyosin
, tropomyosin 3 alpha
, alpha-skeletal tropomyosin
, cardiomyopathy, hypertrophic 3
, sarcomeric tropomyosin kappa
, tropomyosin 1 (alpha) isoform 1
, tropomyosin 1 (alpha) isoform 2
, tropomyosin 1 (alpha) isoform 3
, tropomyosin 1 (alpha) isoform 4
, tropomyosin 1 (alpha) isoform 5
, tropomyosin 1 (alpha) isoform 6
, tropomyosin 1 (alpha) isoform 7
, tropomyosin 1-1
, tropomyosin 1 (alpha)