- Title
- Phosphorylation of Ser¹⁹ alters the conformation of tyrosine hydroxylase to increase the rate of phosphorylation of Ser⁴⁰
- Creator
- Bevilaqua, Lia R. M.; Graham, Mark E.; Dunkley, Peter R.; von Nagy-Felsobuki, Ellak I.; Dickson, Phillip W.
- Relation
- The Journal of Biological Chemistry Vol. 276, Issue 44, p. 40411-40416
- Publisher Link
- http://dx.doi.org/10.1074/jbc.M105280200
- Publisher
- American Society for Biochemistry and Molecular Biology
- Resource Type
- journal article
- Date
- 2001
- Description
- 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 Ser¹⁹ and Ser⁴⁰ produced a TH molecule with a more open conformation than the non-phosphorylated form. The conformational effect of Ser¹⁹ phosphorylation is less pronounced than that of the Ser⁴⁰ phosphorylation. The effect of Ser¹⁹ and Ser⁴⁰ phosphorylation appears to be additive. Binding of dopamine produced a more compact form when compared with the non-dopamine-bound TH. The interdependence of Ser¹⁹ and Ser⁴⁰ phosphorylation was probed using electrospray ionization mass spectrometry. The rate constants for the phosphorylation of Ser¹⁹ and Ser⁴⁰ were determined by electrospray ionization mass spectrometry using a consecutive reaction model. The rate constant for the phosphorylation of Ser⁴⁰ is ~2- to 3-fold higher if Ser¹⁹ is already phosphorylated. These results suggest that phosphorylation of Ser¹⁹ alters the conformation of tyrosine hydroxylase to allow increased accessibility of Ser⁴⁰ to kinases.
- Subject
- phosphorylation; tyrosine hydroxylase; Ser¹⁹; Ser⁴⁰
- Identifier
- uon:1973
- Identifier
- http://hdl.handle.net/1959.13/27751
- Identifier
- ISSN:0021-9258
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