title: Susceptibility of the prion protein to enzymic phosphorylation.
abstract: 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.
authors.affiliation: Dipartimento di Chimica Biologica and Centro CNR di Studio delle Biomembrane, Università di Padova, Viale G. Colombo 3, Padua, 35121, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Negro
authors.forename: F
authors.initials: F
authors.lastname: Meggio
authors.forename: A
authors.initials: A
authors.lastname: Bertoli
authors.forename: R
authors.initials: R
authors.lastname: Battistutta
authors.forename: M C
authors.initials: MC
authors.lastname: Sorgato
authors.forename: L A
authors.initials: LA
authors.lastname: Pinna
mesh_terms: D000818:Animals; D047390:Casein Kinase II; D002417:Cattle; D002942:Circular Dichroism; D003902:Detergents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D010766:Phosphorylation; D010957:Plasmids; D011328:Prions / Q000378:metabolism*; D020033:Protein Isoforms; D011493:Protein Kinase C / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D013696:Temperature; D013997:Time Factors
chemical_list: D003902:Detergents; D011328:Prions; D020033:Protein Isoforms; D011994:Recombinant Proteins; D012694:Serine; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C