▁at ▁the ▁site ▁of ▁integr in ▁binding . ▁Vin cul in ' s ▁ability ▁to ▁interact ▁with ▁integr ins ▁to ▁the ▁c yt os ke leton ▁at ▁the ▁foc al ▁ad hes ion ▁appears ▁to ▁be ▁critical ▁for ▁control ▁of ▁c yt os ke let al ▁mechan ics , ▁cell ▁spread ing , ▁and ▁l am el lip odia ▁formation . ▁Thus , ▁vin cul in ▁appears ▁to ▁play ▁a ▁key ▁role ▁in ▁shape ▁control ▁based ▁on ▁its ▁ability ▁to ▁mod ulate ▁foc al ▁ad hes ion ▁structure ▁and ▁function . ▁ ▁Activ ation ▁ ▁Vin cul in ▁is ▁present ▁in ▁equilibrium ▁between ▁an ▁active ▁and ▁in active ▁state . ▁The ▁active ▁state ▁is ▁triggered ▁upon ▁binding ▁to ▁its ▁designated ▁partner . ▁These ▁changes ▁occur ▁when ▁vin cul in ▁interact s ▁with ▁foc al ▁ad hes ion ▁points ▁to ▁which ▁it ▁is ▁binding ▁to . ▁When ▁vin cul in ▁res ides ▁in ▁its ▁in active ▁form , ▁the ▁protein ▁is ▁kept ▁designated ▁to ▁the ▁cy top las m ▁unlike ▁the ▁foc al ▁ad hes ion ▁points ▁bound ▁from ▁the ▁active ▁state . ▁The ▁mole c ule ▁tal in ▁is ▁thought ▁to ▁be ▁the ▁major ▁initi ator ▁of ▁vin cul in ▁activation ▁due ▁to ▁its ▁presence ▁in ▁foc al ▁complex es . ▁The ▁combin atorial ▁model ▁of ▁vin cul in ▁states ▁that ▁either ▁α - act in in ▁or ▁tal in ▁can ▁activ ate ▁vin cul in ▁either ▁alone ▁or ▁with ▁the ▁assistance ▁of ▁P IP 2 ▁or ▁act in . ▁This ▁activation ▁takes