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Talin-1 induces proliferation and migration of vascular smooth muscle cells obtained from patients with thoracic aortic dissection.
Here, the authors show that cortical microtubule stabilization sites containing CLASPs, KIF21A, LL5beta and liprins are recruited to focal adhesions by the adaptor protein KANK1, which directly interacts with the major adhesion component, talin. Structural studies showed that the conserved KN domain in KANK1 binds to the talin rod domain R7.
Vinculin (show VCL Proteins) head-tail interaction is required on soft substrates to destabilize vinculin (show VCL Proteins) and talin in FAs (show FAS Proteins), and to allow hMSCs branching. Another module involves paxillin (show PXN Proteins) and FAK (show PTK2 Proteins), which soft substrates also destabilize, but independently of vinculin (show VCL Proteins) head-tail interaction. This multi-modularity may be key to allow a versatile response to complex biomechanical cues.
The central role of talin and vinculin (show VCL Proteins) 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 (show MMRN1 Proteins) interactions and remodeling of the tissue.
Application of these techniques to new talin biosensors reveals an intramolecular tension gradient across talin-1 that is established upon integrin-mediated cell adhesion. The tension gradient is actomyosin- and vinculin (show VCL Proteins)-dependent and sensitive to the rigidity of the extracellular environment
Our findings confirm the role of Talin-1 in carcinogenesis and provided a set of novel therapeutic targets for the treatment of hepatocellular carcinoma
These data show that TLN1 can act as a viral restriction factor that suppresses hepatitis B virus replication, and suggest that the HBx relieves this restriction by inducing TLN1 degradation.
The ERK (show EPHB2 Proteins) pathway was responsible for these promoting effects of Talin1 knockdown in HCC (show FAM126A Proteins) cells.
This study showed that serum sTalin-1 levels were associated with a sustained increase in disability after MS attack but not with serum anti-Talin-1 antibody levels.
The Rap1 (show RABGEF1 Proteins)-RIAM (show APBB1IP Proteins)-talin axis of integrin activation and blood cell function
Loss of all Tln forms from the heart-muscle cell leads to myocyte instability and a dilated cardiomyopathy.
SKAP1 (show SKAP1 Proteins) can affect the function of talin in T-cells needed for optimal T-cell/dendritic cell conjugation
FAK sustained the active integrin conformation by maintaining talin association with Rab11 endosomes in a type I phosphatidylinositol phosphate kinase (PIPKIgamma)-dependent manner.
These findings show that talin and kindlin cooperatively activate integrins leading to fibronectin (show FN1 Proteins) binding and adhesion.
Binding of vinculin (show VCL Proteins) 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 (show TLN2 Proteins) modulates extracellular rigidity sensing.
Conformational activation of talin by PREL-1 (show APBB1IP Proteins) triggers integrin-mediated cell adhesion.
Direct methylation of talin, a key regulatory molecule in cell migration, by Ezh2 disrupted the binding of talin to F-actin and thereby promoted the turnover of adhesion structures.
reduction of talin-beta3 integrin (show ITGB3 Proteins) binding affinity results in decelerated alphaIIbbeta3 integrin activation and protection from arterial thrombosis without pathological bleeding
As talin engages F-actin, force exerted on the R2R3 helical bundles disrupts RIAM (show APBB1IP Proteins) binding and exposes the vinculin (show VCL Proteins) binding sites, which recruit vinculin (show VCL Proteins) to stabilize the complex.
suggest that Tln1-mediated Itgbeta1b plays a crucial role in maintaining cardiac sarcomeric Z-disks and endothelial/endocardial cell integrity in zebrafish
CD90 (Thy1 (show THY1 Proteins)) is a novel interactor of talin 1 in effector cells of autoimmune equine uveitis.
This gene encodes a cytoskeletal protein that is concentrated in areas of cell-substratum and cell-cell contacts. The encoded protein plays a significant role in the assembly of actin filaments and in spreading and migration of various cell types, including fibroblasts and osteoclasts. It codistributes with integrins in the cell surface membrane in order to assist in the attachment of adherent cells to extracellular matrices and of lymphocytes to other cells. The N-terminus of this protein contains elements for localization to cell-extracellular matrix junctions. The C-terminus contains binding sites for proteins such as beta-1-integrin, actin, and vinculin.
, talin 1
, Talin 1