▁and ▁DE P ▁domains . ▁When ▁a ▁W nt ▁mole c ule ▁bind s ▁to ▁Fri zz led , ▁it ▁indu ces ▁a ▁poor ly ▁known ▁cas cade ▁of ▁events , ▁that ▁result ▁in ▁the ▁expos ure ▁of ▁dis he vel led ' s ▁D IX ▁domain ▁and ▁the ▁creation ▁of ▁a ▁perfect ▁binding ▁site ▁for ▁ax in . ▁Ax in ▁is ▁then ▁tit r ated ▁away ▁from ▁its ▁o lig omer ic ▁assemb lies ▁– ▁the ▁ β - c aten in ▁destruction ▁complex ▁– ▁by ▁D sh . ▁Once ▁bound ▁to ▁the ▁re ceptor ▁complex , ▁ax in ▁will ▁be ▁rendered ▁in comp et ent ▁for ▁ β - c aten in ▁binding ▁and ▁G SK 3 ▁activity . ▁Import antly , ▁the ▁cy top las mic ▁segments ▁of ▁the ▁Fri zz led - associ ated ▁L R P 5 ▁and ▁L R P 6 ▁prote ins ▁contain ▁G SK 3 ▁pseudo - substr ate ▁sequences ▁( Pro - Pro - Pro - Ser - Pro - x - Ser ), ▁appropri ately ▁" prim ed " ▁( pre - ph osph ory l ated ) ▁by ▁C K I , ▁as ▁if ▁it ▁were ▁a ▁true ▁substr ate ▁of ▁G SK 3 . ▁These ▁false ▁target ▁sites ▁greatly ▁in hib it ▁G SK 3 ▁activity ▁in ▁a ▁compet itive ▁manner . ▁ ▁This ▁way ▁re ceptor - bound ▁ax in ▁will ▁abol ish ▁medi ating ▁the ▁ph osph ory lation ▁of ▁ β - c aten in . ▁Since ▁beta