the close relationship of dmpk to the rho-kinases has led to speculation whether dmpk activity may be regulated in vivo by small g proteins, particularly of the rho family. although dmpk lacks obvious binding sites for known g, dmpk-1 oligomers exhibit low basal catalytic activity due to the presence of the c-terminal autoinhibitory domain (ai). a protease (p) within the membrane cleaves dmpk-1, removing the c-terminal autoinhibitory and membrane association domains and releasing cytosolic, basally active dmpk-2. this processing event would produce longterm activation of the kinase. short-term activation of dmpk-1 and -2 may be mediated by transitory interaction with a small gtpase (g).