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

doi:10.1016/0014-5793(89)81424-3

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

MRC PPU

Research output: Contribution to journal › Article › peer-review

103 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 language	English
Pages (from-to)	36-42
Number of pages	7
Journal	FEBS Letters
Volume	251
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(89)81424-3
Publication status	Published - 17 Jul 1989

Keywords

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

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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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 = jul,

day = "17",

doi = "10.1016/0014-5793(89)81424-3",

language = "English",

volume = "251",

pages = "36--42",

journal = "FEBS Letters",

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T1 - Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum

T2 - evidence from the effects of okadaic acid

AU - Haavik, Jan

AU - Schelling, Donald L.

AU - Campbell, David G.

AU - Andersson, Kristoffer K.

AU - Flatmark, Torgeir

AU - Cohen, Philip

PY - 1989/7/17

Y1 - 1989/7/17

N2 - (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.

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.

KW - Calmodulin

KW - cyclic AMP

KW - Okadaic acid

KW - Protein kinase

KW - Protein phosphatase

KW - Protein sequencing

KW - Tyrosine hydroxylase

UR - https://www.scopus.com/pages/publications/0024309434

U2 - 10.1016/0014-5793(89)81424-3

DO - 10.1016/0014-5793(89)81424-3

M3 - Article

C2 - 2568951

AN - SCOPUS:0024309434

SN - 0014-5793

VL - 251

SP - 36

EP - 42

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Keywords

ASJC Scopus subject areas

Access to Document

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