Glycogenin, the primer of glycogen synthesis, binds to actin.

ABSTRACT

We have studied the intracellular localization of glycogenin by fusing green fluorescent protein (GFP) to the N-terminus of rabbit muscle glycogenin and expressing the chimeric protein in C2C12, COS-1 and rat hepatic cells. The fusion protein showed a nuclear and cytosolic distribution and partially co-localized with actin in the cytosol. Disruption of the actin cytoskeleton with cytochalasin D led to a change in the pattern of green fluorescence, which coincided with that observed for the remaining non-depolymerized actin. The distribution of the single point mutant K324A was completely uniform and was not affected by this drug. These findings indicate that rabbit muscle glycogenin binds to actin through the heptapeptide 321DNIKKKL327, a common motif found in other actin-binding proteins, which is located at the C-terminal end of this protein, and suggest that the actin cytoskeleton plays an important role in glycogen metabolism.