Partial Structure of the Mouse Glucokinase Gene

Ishimura-Oka, Kazumi; Nakamuta, Makoto; Chu, Mei-jin; Sullivan, Merry; Chan, Lawrence; Oka, Koichiro

doi:10.1006/geno.1995.9942

Cited by 6 publications

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…More interestingly, the glucokinases characterized from rat [32], mouse [33]and human [34]tissues all contain the DAIKRR sequence, again highly homologous to that found in actin‐binding proteins as well as in glycogenin. Rat glucokinase from liver and islet pancreatic β‐cells, overexpressed in COS‐7 cells, as well as endogenous rat liver glucokinase have been shown to co‐localize with actin filaments [35].…”

Section: Discussionmentioning

confidence: 99%

Glycogenin, the primer of glycogen synthesis, binds to actin

1997

View full text Add to dashboard Cite

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 C 2 Ci 2 , 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 321 DNIKKKL 327 , 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.

show abstract

Section: Discussionmentioning

confidence: 99%