vinculin การใช้

• Vinculin is a 117-kDa cytoskeletal protein with 1066 amino acids.
• Vinculin is a large protein of 116 kDa ( about a 1000 residues ).
• Alpha-catenins are evolutionary related to vinculin.
• The amino acid sequence of alpha-catenin has sequence similarity to that of vinculin.
• Alpha-catenins are proteins of about 100 kDa which are evolutionary related to vinculin.
• Metavinculin tail domain has a lower affinity for the head as compared with the vinculin tail.
• The binding of vinculin to talin and actin is regulated by polyphosphoinositides and inhibited by acidic phospholipids.
• Recently, ?-catenin has been shown to associate with formins, EPLIN, and vinculin.
• The adherens junctions consist of large number of proteins including ?-actinin, vinculin and cytoskeletal actin.
• Talin also binds with high affinity to vinculin, another cytoskeletal protein concentrated at points of cell adhesion.
• Its splice variant metavinculin ( see below ) also needs vinculin to heterodimerize and work in a dependent fashion.
• This transformation elicited the relocalization of vinculin and ?-actin in the cytoskeleton from focal adhesions forming circular clusters.
• For example, vinculin is able to control the cell s motility by simply altering its shape from active to inactive.
• The vinculin gene occurs as a single copy and what appears to be no close relative to take over functions in its absence.
• Thus, vinculin appears to play a key role in shape control based on its ability to modulate focal adhesion structure and function.
• Binding alternately to talin or ?-actinin, vinculin's shape and, as a consequence, its binding properties are changed.
• The loss of vinculin impacts a variety of cell functions; it disrupts the formation of the complex, and prevents cell adhesion and spreading.
• Based on research, it has been postulated that the lack of vinculin may decrease cell adhesion by inhibiting focal adhesion assembly and preventing actin polymerization.
• Within the cell, the intracellular domain of integrin binds to the cytoskeleton via adapter proteins such as ?-actinin, filamin, vinculin and tensin.
• EPLIN has been found to enhance the bundling and stabilization of actin filaments, and vinculin is involved in the linkage of adhesion molecules to the actin cytoskeleton.