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VCL/Vinculin  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: Human Cells  
  • Slide 1
50 µg 
20 µg 
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Expression host: Human Cells  
  • Slide 1
20 µg 
10 µg 
Add to Cart

VCL/Vinculin Related Area

VCL/Vinculin Related Pathways

    VCL/Vinculin Summary & Protein Information

    VCL/Vinculin Background

    Gene Summary: Vinculin is a cytoskeletal protein associated with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. Defects in VCL are the cause of cardiomyopathy dilated type 1W. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Multiple alternatively spliced transcript variants have been found for this gene, but the biological validity of some variants has not been determined.
    General information above from NCBI
    Subunit structure: Exhibits self-association properties. Interacts with APBB1IP, NRAP and SORBS1 (By similarity). Interacts with TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin (By similarity). Interacts with SYNM. {ECO:0000250, ECO:0000269|PubMed:14702644, ECO:0000269|PubMed:15070891, ECO:0000269|PubMed:18028034}.
    Domain: Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion. {ECO:0000269|PubMed:20484056}.; The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. In isoform 2 (metavinculin) a 68 residue insertion in the tail domain promotes actin severing instead of bundling. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly. {ECO:0000269|PubMed:20484056}.
    Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18439753}. Cell junction, adherens junction {ECO:0000269|PubMed:18439753}. Cell membrane {ECO:0000269|PubMed:18439753}; Peripheral membrane protein {ECO:0000269|PubMed:18439753}; Cytoplasmic side {ECO:0000269|PubMed:18439753}. Cell junction, focal adhesion {ECO:0000269|PubMed:18439753}. Note=Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions (By similarity). Colocalizes with LIMD1 in the focal adhesions. {ECO:0000250}.
    Tissue specificity: Metavinculin is muscle-specific.
    Post-translational: Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity). {ECO:0000250}.; Acetylated; mainly by myristic acid but also by a small amount of palmitic acid. {ECO:0000250}.
    Involvement in disease: DISEASE: Cardiomyopathy, dilated 1W (CMD1W) [MIM:611407]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269|PubMed:11815424, ECO:0000269|PubMed:16236538}. Note=The disease is caused by mutations affecting the gene represented in this entry.; DISEASE: Cardiomyopathy, familial hypertrophic 15 (CMH15) [MIM:613255]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. {ECO:0000269|PubMed:16712796}. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Belongs to the vinculin/alpha-catenin family. {ECO:0000305}.
    General information above from UniProt

    Vinculin (VCL) is a cytoskeletal protein that is closely related to both cell-matrix interactions and cell-cell junctions. VCL is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. The protein contains an acidic N-terminal domain and a basic C-terminal domain separated by a proline-rich middle segment. This protein has multi-ligand properties and has been found to interact with a number of microfilament associated proteins, such as talin, a-actinin, and paxillin, which reportedly bind to either the head or tail domains of vinculin.

    VCL/Vinculin Alternative Name

    MV,MVCL,CMD1W,CMH15,HEL114, [homo-sapiens]
    CMD1W,CMH15,MVCL,RP11-178G16.3, [human]
    9430097D22,AA571387,AI462105,AW545629, [mouse]
    AA571387,AI462105,AW545629,9430097D22, [mus-musculus]

    VCL/Vinculin Related Studies

  • Massoumi R, et al. (2001) Leukotriene D(4) affects localisation of vinculin in intestinal epithelial cells via distinct tyrosine kinase and protein kinase C controlled events. J Cell Sci. 114(10): 1925-34.
  • Turner CE, et al. (1994) Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J Cell Sci. 107 (6): 1583-91.
  • Strasser P, et al. (1993) Variable and constant regions in the C-terminus of vinculin and metavinculin: cloning and expression of fragments in E. coli. FEBS Lett. 317: 189-194.