Vinculin
Sign in to saveAlso known as epididymis secretory sperm binding protein, epididymis luminal protein 114, metavinculin, VCL, meta-vinculin, MV
thumb|Vinculin is a globular protein approximately 115 x 85 x 65 angstroms in linear dimension. In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. 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.
Key facts
- Protein family.Symbol
- VBS
- Protein family.Name
- VBS
- Protein family.image
- PDB 1rkc EBI.jpg
- Protein family.caption
- human vinculin head (1-258) in complex with talin's vinculin binding site 3 (residues 1944-1969)
- Protein family.Pfam
- PF08913
- Protein family.InterPro
- IPR015009
via Wikipedia infobox
Protein · UniProt
Vinculin
- Gene
- VCL
- Organism
- Homo sapiens (Human)
- Length
- 1,134 aa
- Molecular mass
- 123,799 Da
- Evidence
- 1: Evidence at protein level
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
Swiss-Prot (reviewed) · via UniProt
~8 min read
Article
9 sectionsContents
- Structure
- Mechanism and function
- Activation
- Binding site
- Splice variants
- Interactions
- References
- Further reading
- External links
thumb|Vinculin is a globular protein approximately 115 x 85 x 65 angstroms in linear dimension. In mammalian cells, vinculin is a membrane-cytoskeletal protein in focal adhesion plaques that is involved in linkage of integrin adhesion molecules to the actin cytoskeleton. 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.
Discovered independently by Benny Geiger and Keith Burridge, its sequence is 20%–30% similar to α-catenin, which serves a similar function.