VCL
GeneName
VCL
Summary
VCL, also known as vinculin or metavinculin, is a 124kDa cytoskeletal protein that plays a pivotal role in cell adhesion and mechanotransduction. It is primarily localised at cell-cell junctions and focal adhesions, where it interacts with various proteins such as cadherins and integrins, facilitating the connection between the cytoskeleton and the plasma membrane. VCL is involved in the assembly of adherens junctions and is crucial for maintaining the structural integrity of tissues, particularly in epithelial and muscle cells. Its functions extend to actin binding and serving as a molecular adaptor, linking various signalling pathways and structural components within the cell.
Importance
VCL is relevant to: - The maintenance of tissue architecture and integrity through its role in cell adhesion and junction assembly. - Mechanotransduction processes, which are essential for cellular responses to mechanical stimuli, influencing cell behaviour and fate. - The regulation of the blood-brain barrier, impacting neurological health and disease. - Muscle function and development due to its presence in costameres and sarcomeres, which are vital for muscle fibre integrity and contraction.
Top Products
For researchers investigating VCL, we highly recommend the top-selling recombinant antibody, Anti-Vinculin antibody [EPR8185] (ab129002). This antibody is well-cited, with 491 citations, reflecting its strong reputation in the field. It has been validated in knockout models and is suitable for a variety of applications, including Western blotting (WB), immunocytochemistry (ICC), immunoprecipitation (IP), and flow cytometry (FC). This versatility makes it an excellent choice for reliable detection of Vinculin in your experiments.
Abcam Product Citation Summary
The data indicates that the VCL antibody (ab129002) is widely used in various studies involving human and mouse models, particularly in the context of cancer research, apoptosis, and cellular stress responses. The antibody is frequently employed in Western blotting to assess protein expression levels across different cell types and conditions, highlighting its importance in understanding cellular mechanisms and disease states.
Abcam Product Citation Table
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.
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.
Function
Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Involvement in disease
Cardiomyopathy, dilated, 1W
CMD1W
A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
None
The disease is caused by variants affecting the gene represented in this entry.
Cardiomyopathy, familial hypertrophic, 15
CMH15
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.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
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).
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.
Sequence Similarities
Belongs to the vinculin/alpha-catenin family.
Tissue Specificity
Metavinculin is muscle-specific.
Cellular localization
- Cell membrane
- Peripheral membrane protein
- Cytoplasmic side
- Cell junction
- Adherens junction
- Cell junction
- Focal adhesion
- Cytoplasm
- Cytoskeleton
- Cell membrane
- Sarcolemma
- Peripheral membrane protein
- Cytoplasmic side
- Cell projection
- Podosome
- Cytoplasm
- Perinuclear region
- 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.
Alternative names
Vinculin, Metavinculin, MV, VCL