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These results showed that difference in the expression pattern and location of miR-126-3p occurred at different stages of the bovine corpus luteum and that miR-126-3p is an important regulator of talin2 (TLN2).
The central role of talin and vinculin in cell adhesions suggests that the disintegration of the tissue in atherosclerosis could be partially driven by downregulation of these genes, leading to loosening of cell-ECM interactions and remodeling of the tissue.
These results suggest that a strong interaction of talin2 with integrins is required to generate traction, which in turn drives invadopodium-mediated matrix degradation, which is key to cancer cell invasion.
data suggest a potential molecular link between TLN2 and camptodactyly pathogenesis.
Both TLN-1 and TLN-2 levels correlate with tumorigenicity in human HCC, indicating that these molecules constitute important molecular targets for the diagnosis and/or treatment of hepatocellular carcinoma .
Data indicate the role of vinculin in inducing the talin mediated integrin activation.
Talin1 has unique expression versus talin 2 in the heart and modifies the hypertrophic response to pressure overload.
Data show that SCGB3A1 was down-regulated in invasive compared with DCIS, whereas talin 2 (TLN2) and PTGS1 were up-regulated in invasive compared with DCIS.
This review discusses the general function of talin 1 and talin 2, as well as vinculin/metavinulin, with emphasis on what is understood about their role in the cardiac myocyte and in whole heart.
Structural diversity in integrin/talin interactions.
the differential concentration of CSF and serum-talin 2 in the drug-refractory postencephalitic epilepsy group is an intractability-related phenomenon that might be involved in the development of RPEE
we show that the predominant brain splice variant of PtdInsPKI gamma (PtdInsPKI gamma-90) binds, by means of a short carboxy-terminal peptide, to the FERM domain of talin, and is strongly activated by this interaction
The F-actin binding capacity of Talin 2 is regulated by intrasteric occlusion of primary actin-binding determinants within the talin I/LWEQ module.
Talin2 may serve as the link between integrins and the sarcomeric cytoskeletonin stable adhesion complexes in mature striated muscle.
Data show that TLN2n presents only in the CSF of temporal lobe epilepsy patients.
Loss of all Tln forms from the heart-muscle cell leads to myocyte instability and a dilated cardiomyopathy.
Binding of vinculin to the R1-R3 region of the talin rod is important for focal adhesion stability.
Data indicate that talin mechanics are isoform specific so that expression of either talin-1 or talin-2 modulates extracellular rigidity sensing.
Tln2(cd/cd) mice showed no major difference in body mass or the weight of the major organs compared to wild-type, although they displayed a mildly dystrophic phenotype.
Talin1 was concentrated in peripheral focal adhesions while talin2 was observed in both focal and fibrillar adhesions, and knock-down of talin2 compromised fibronectin fibrillogenesis
Fxr1 knockout hearts exhibit an up-regulation of desmoplakin and talin2 proteins, which is accompanied by severe disruption of desmosome as well as costamere architecture and composition in the heart
Depletion of talin2 in talin1-null cells did not affect the initiation of matrix-activated spreading or Src family kinase activation, but abolished the extracellular matrix-integrin-cytoskeleton linkage, sustained cell spreading and adhesion.
demonstrate that testis and kidney express truncated talin 2 isoforms that lack the N-terminal half of the protein, and provide evidence for the developmentally regulated expression of the short testis-specific talin 2 isoform in elongating spermatids
Talin 1 and 2 are crucial for skeletal muscle development, where they regulate myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions.
Data show that clustered alpha(5)beta(1) integrins, while less stable links to alpha(v)beta(3) integrins initiate mechanotransduction, resulting in reinforcement of integrin-cytoskeleton linkages through talin-dependent bonds.
This gene encodes a protein related to talin 1, a cytoskeletal protein that plays a significant role in the assembly of actin filaments and in spreading and migration of various cell types, including fibroblasts and osteoclasts. This protein has a different pattern of expression compared to talin 1 but, like talin 1, is thought to associate with unique transmembrane receptors to form novel linkages between extracellular matrices and the actin cytoskeleton.