P. Keller et al., PHOSPHORYLATION OF THE N-TERMINAL INTRACELLULAR TAIL OF SUCRASE-ISOMALTASE BY CAMP-DEPENDENT PROTEIN-KINASE, European journal of biochemistry, 233(3), 1995, pp. 963-968
This paper reports the phosphorylation of the intracellular N-terminal
tail of sucrase-isomaltase by protein kinase A and shows that this ph
osphorylation is targeted to Ser6 within a sequence Arg/Lys/Lys-Phe-Se
r, which is conserved in all sucrase-isomaltase sequences known so far
. By dephosphorylation of native sucrase-isomaltase with an immobilize
d acid phosphatase and rephosphorylation with protein kinase A, it is
shown that Ser6 may be partially phosphorylated in vivo, raising the p
ossibility that the tail itself and its phosphorylation by protein kin
ase A may be physiologically significant.