ADP-Ribosylation of the Intermediate Filament Protein Desmin and Inhibition of Desmin Assembly in Vitroby Muscle ADP-Ribosyltransferase

Autor: Huang, H.Y., Graves, D.J., Robson, R.M., Huiatt, T.W.
Zdroj: Biochemical and Biophysical Research Communications; December 1993, Vol. 197 Issue: 2 p570-577, 8p
Abstrakt: Arginine-specific mono(ADP-ribosyl)transferase purified from rabbit skeletal muscle catalyzes stoichiometric ADP-ribosylation of the intermediate filament protein, desmin. In contrast, choleratoxin catalyzes a much lower level of ADP-ribosylation of desmin. Modification results in potent inhibition of desmin′s ability to assemble into filaments. Phosphorylation of desmin by the catalytic subunit of cAMP dependent protein kinase is also inhibited by ADP-ribosylation. ADP-ribosylation site(s) are located within the N-terminal head domain of desmin.
Databáze: Supplemental Index