Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum

evidence from the effects of okadaic acid

Jan Haavik, Donald L. Schelling, David G. Campbell, Kristoffer K. Andersson, Torgeir Flatmark, Philip Cohen

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

(i) The major sites on bovine adrenal tyrosine hydroxylase (TH) phosphorylated by calmodulin-dependent multiprotein kinase (CaM-MPK) and cyclic AMP-dependent protein kinase were shown to be Ser-19 and Ser-40, respectively, while Ser-40 was also phosphorylated slowly by CAM-MPK. (ii) Type 2A and type 2C phosphatases accounted for ≈90% and ≈ 10% of TH phosphatase activity, respectively, in extracts of adrenal medulla and corpus striatum assayed at near physiological free Mg2+(1 mM), while type 1 and type 2B phosphatases had negligible activity towards TH. (iii) Incubation of adrenal chromaffin cells with okadaic acid increased TH phosphorylation by 206% and activity by 77%, establishing that type 2A phosphatases play a major role in regulating TH in vivo.

Original languageEnglish
Pages (from-to)36-42
Number of pages7
JournalFEBS Letters
Volume251
Issue number1-2
DOIs
Publication statusPublished - 17 Jul 1989

Fingerprint

Corpus Striatum
Protein Phosphatase 2
Okadaic Acid
Adrenal Medulla
Tyrosine 3-Monooxygenase
Phosphoric Monoester Hydrolases
Chromaffin Cells
Calcium-Calmodulin-Dependent Protein Kinases
Phosphorylation
Computer aided manufacturing
Cyclic AMP-Dependent Protein Kinases

Keywords

  • Calmodulin
  • cyclic AMP
  • Okadaic acid
  • Protein kinase
  • Protein phosphatase
  • Protein sequencing
  • Tyrosine hydroxylase

Cite this

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title = "Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid",
abstract = "(i) The major sites on bovine adrenal tyrosine hydroxylase (TH) phosphorylated by calmodulin-dependent multiprotein kinase (CaM-MPK) and cyclic AMP-dependent protein kinase were shown to be Ser-19 and Ser-40, respectively, while Ser-40 was also phosphorylated slowly by CAM-MPK. (ii) Type 2A and type 2C phosphatases accounted for ≈90{\%} and ≈ 10{\%} of TH phosphatase activity, respectively, in extracts of adrenal medulla and corpus striatum assayed at near physiological free Mg2+(1 mM), while type 1 and type 2B phosphatases had negligible activity towards TH. (iii) Incubation of adrenal chromaffin cells with okadaic acid increased TH phosphorylation by 206{\%} and activity by 77{\%}, establishing that type 2A phosphatases play a major role in regulating TH in vivo.",
keywords = "Calmodulin, cyclic AMP, Okadaic acid, Protein kinase, Protein phosphatase, Protein sequencing, Tyrosine hydroxylase",
author = "Jan Haavik and Schelling, {Donald L.} and Campbell, {David G.} and Andersson, {Kristoffer K.} and Torgeir Flatmark and Philip Cohen",
year = "1989",
month = "7",
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doi = "10.1016/0014-5793(89)81424-3",
language = "English",
volume = "251",
pages = "36--42",
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Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum : evidence from the effects of okadaic acid. / Haavik, Jan; Schelling, Donald L.; Campbell, David G.; Andersson, Kristoffer K.; Flatmark, Torgeir; Cohen, Philip.

In: FEBS Letters, Vol. 251, No. 1-2, 17.07.1989, p. 36-42.

Research output: Contribution to journalArticle

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AB - (i) The major sites on bovine adrenal tyrosine hydroxylase (TH) phosphorylated by calmodulin-dependent multiprotein kinase (CaM-MPK) and cyclic AMP-dependent protein kinase were shown to be Ser-19 and Ser-40, respectively, while Ser-40 was also phosphorylated slowly by CAM-MPK. (ii) Type 2A and type 2C phosphatases accounted for ≈90% and ≈ 10% of TH phosphatase activity, respectively, in extracts of adrenal medulla and corpus striatum assayed at near physiological free Mg2+(1 mM), while type 1 and type 2B phosphatases had negligible activity towards TH. (iii) Incubation of adrenal chromaffin cells with okadaic acid increased TH phosphorylation by 206% and activity by 77%, establishing that type 2A phosphatases play a major role in regulating TH in vivo.

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