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Titolo:
Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylaseto increase the rate of phosphorylation of Ser(40)
Autore:
Bevilaqua, LRM; Graham, ME; Dunkley, PR; von Nagy-Felsobuki, EI; Dickson, PW;
Indirizzi:
Univ Newcastle, Fac Med & Hlth Sci, Sch Biomed Sci, Callaghan, NSW 2308, Australia Univ Newcastle Callaghan NSW Australia 2308 allaghan, NSW 2308, Australia Univ Newcastle, Sch Biol & Chem Sci, Callaghan, NSW 2308, Australia Univ Newcastle Callaghan NSW Australia 2308 allaghan, NSW 2308, Australia
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 44, volume: 276, anno: 2001,
pagine: 40411 - 40416
SICI:
0021-9258(20011102)276:44<40411:POSATC>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADRENAL CHROMAFFIN CELLS; GLYCOGEN-SYNTHASE KINASE-3; SITE-DIRECTED MUTAGENESIS; MASS-SPECTROMETRY; PROTEIN-KINASE; IDENTIFICATION; ACTIVATION; EXPRESSION; MECHANISM; DOPAMINE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Dickson, PW Univ Newcastle, Fac Med & Hlth Sci, Sch Biomed Sci, Callaghan,NSW 2308, Australia Univ Newcastle Callaghan NSW Australia 2308 W 2308, Australia
Citazione:
L.R.M. Bevilaqua et al., "Phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylaseto increase the rate of phosphorylation of Ser(40)", J BIOL CHEM, 276(44), 2001, pp. 40411-40416

Abstract

The effect of phosphorylation on the shape of tyrosine hydroxylase (TH) was studied directly using gel filtration and indirectly using electrospray ionization mass spectrometry. Phosphorylation of Ser(19) and Ser(40) produced a TH molecule with a more open conformation than the non-phosphorylated form. The conformational effect of Ser(19) phosphorylation is less pronounced than that of the Ser(40) phosphorylation. The effect of Ser(19) and Ser(40) phosphorylation appears to be additive. Binding of dopamine produced a more compact form when compared with the non-dopamine-bound TH. The interdependence of Ser(19) and Ser(40) phosphorylation was probed using electrospray ionization mass spectrometry. The rate constants for the phosphorylation of Ser(19) and Ser(40) were determined by electrospray ionization mass spectrometry using a consecutive reaction model. The rate constant for the phosphorylation of Ser(40) is similar to2 to 3-fold higher if Ser(19) is already phosphorylated. These results suggest that phosphorylation of Ser(19) alters the conformation of tyrosine hydroxylase to allow increased accessibility of Ser(40) to kinases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 19:24:10