NR AIVB
AU Negro,A.; Meggio,F.; Bertoli,A.; Battistutta,R.; Sorgato,M.C.; Pinna,L.A.
TI Susceptibility of the prion protein to enzymic phosphorylation
QU Biochemical and Biophysical Research Communications 2000 May 10; 271(2): 337-41
PT journal article
AB Ten protein kinases have been assayed for their ability to phosphorylate in vitro the recombinant bovine PrP (25-242) (rbPrP). Substantial phosphorylation was observed with PKC, CK2, and two tyrosine kinases, Lyn and c-Fgr. With regard to CK2, phosphorylation occurs at Ser 154 with a stoichiometry of about 0.1 mol phosphate/mol rbPrP, which is doubled by mild heat treatment of rbPrP. Heat also reduces the overall protein ellipticity, suggesting that reversibly unfolded conformers are more susceptible to phosphorylation. Our data disclose the possibility that phosphorylation might modulate PrP biological activity.
MH Animal; Cattle; Circular Dichroism; Detergents/pharmacology; Electrophoresis, Polyacrylamide Gel; Mice; Phosphorylation; Plasmids; Prions/*metabolism; Protein Isoforms; Protein Kinase C/metabolism; Protein-Serine-Threonine Kinases/metabolism; Recombinant Proteins/metabolism; Serine/metabolism; Support, Non-U.S. Gov't; Temperature; Time Factors
AD Dipartimento di Chimica Biologica and Centro CNR di Studio delle Biomembrane, Universita di Padova, Viale G. Colombo 3, Padua, 35121, Italy.
SP englisch
PO USA