Phosphorylation of mouse serine racemase regulates D-serine synthesis

Veronika N Foltyn, Martin Zehl, Elena Dikopoltsev, Ole N Jensen, Herman Wolosker

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Serine racemase (SR) catalyses the synthesis of the transmitter/neuromodulator D-serine, which plays a major role in synaptic plasticity and N-methyl D-aspartate receptor neurotoxicity. We now report that SR is phosphorylated at Thr71 and Thr227 as revealed by mass spectrometric analysis and in vivo phosphorylation assays. Thr71 phosphorylation was observed in the cytosolic and membrane-bound SR while Thr227 phosphorylation was restricted to the membrane fraction. The Thr71 site has a motif for proline-directed kinases and is the main phosphorylation site of SR. Experiments with a phosphorylation-deficient SR mutant indicate that Thr71 phosphorylation increases SR activity, suggesting a novel mechanism for regulating D-serine production.
OriginalsprogEngelsk
TidsskriftFEBS letters
Vol/bind584
Udgave nummer13
Sider (fra-til)2937-41
Antal sider4
DOI
StatusUdgivet - 2. jul. 2010

Fingeraftryk

Phosphorylation
Serine
Membranes
N-Methyl-D-Aspartate Receptors
Proline
Plasticity
Neurotransmitter Agents
serine racemase
Transmitters
Assays
Phosphotransferases
Experiments

Citer dette

Foltyn, Veronika N ; Zehl, Martin ; Dikopoltsev, Elena ; Jensen, Ole N ; Wolosker, Herman. / Phosphorylation of mouse serine racemase regulates D-serine synthesis. I: FEBS letters. 2010 ; Bind 584, Nr. 13. s. 2937-41.
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abstract = "Serine racemase (SR) catalyses the synthesis of the transmitter/neuromodulator D-serine, which plays a major role in synaptic plasticity and N-methyl D-aspartate receptor neurotoxicity. We now report that SR is phosphorylated at Thr71 and Thr227 as revealed by mass spectrometric analysis and in vivo phosphorylation assays. Thr71 phosphorylation was observed in the cytosolic and membrane-bound SR while Thr227 phosphorylation was restricted to the membrane fraction. The Thr71 site has a motif for proline-directed kinases and is the main phosphorylation site of SR. Experiments with a phosphorylation-deficient SR mutant indicate that Thr71 phosphorylation increases SR activity, suggesting a novel mechanism for regulating D-serine production.",
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author = "Foltyn, {Veronika N} and Martin Zehl and Elena Dikopoltsev and Jensen, {Ole N} and Herman Wolosker",
note = "Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",
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Foltyn, VN, Zehl, M, Dikopoltsev, E, Jensen, ON & Wolosker, H 2010, 'Phosphorylation of mouse serine racemase regulates D-serine synthesis', FEBS letters, bind 584, nr. 13, s. 2937-41. https://doi.org/10.1016/j.febslet.2010.05.022

Phosphorylation of mouse serine racemase regulates D-serine synthesis. / Foltyn, Veronika N; Zehl, Martin; Dikopoltsev, Elena; Jensen, Ole N; Wolosker, Herman.

I: FEBS letters, Bind 584, Nr. 13, 02.07.2010, s. 2937-41.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Phosphorylation of mouse serine racemase regulates D-serine synthesis

AU - Foltyn, Veronika N

AU - Zehl, Martin

AU - Dikopoltsev, Elena

AU - Jensen, Ole N

AU - Wolosker, Herman

N1 - Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

PY - 2010/7/2

Y1 - 2010/7/2

N2 - Serine racemase (SR) catalyses the synthesis of the transmitter/neuromodulator D-serine, which plays a major role in synaptic plasticity and N-methyl D-aspartate receptor neurotoxicity. We now report that SR is phosphorylated at Thr71 and Thr227 as revealed by mass spectrometric analysis and in vivo phosphorylation assays. Thr71 phosphorylation was observed in the cytosolic and membrane-bound SR while Thr227 phosphorylation was restricted to the membrane fraction. The Thr71 site has a motif for proline-directed kinases and is the main phosphorylation site of SR. Experiments with a phosphorylation-deficient SR mutant indicate that Thr71 phosphorylation increases SR activity, suggesting a novel mechanism for regulating D-serine production.

AB - Serine racemase (SR) catalyses the synthesis of the transmitter/neuromodulator D-serine, which plays a major role in synaptic plasticity and N-methyl D-aspartate receptor neurotoxicity. We now report that SR is phosphorylated at Thr71 and Thr227 as revealed by mass spectrometric analysis and in vivo phosphorylation assays. Thr71 phosphorylation was observed in the cytosolic and membrane-bound SR while Thr227 phosphorylation was restricted to the membrane fraction. The Thr71 site has a motif for proline-directed kinases and is the main phosphorylation site of SR. Experiments with a phosphorylation-deficient SR mutant indicate that Thr71 phosphorylation increases SR activity, suggesting a novel mechanism for regulating D-serine production.

KW - Animals

KW - Cell Line

KW - Cell Line, Tumor

KW - Chromatography, Liquid

KW - Humans

KW - Mass Spectrometry

KW - Mice

KW - Phosphorylation

KW - Protein Structure, Secondary

KW - Racemases and Epimerases

KW - Serine

KW - Tandem Mass Spectrometry

U2 - 10.1016/j.febslet.2010.05.022

DO - 10.1016/j.febslet.2010.05.022

M3 - Journal article

VL - 584

SP - 2937

EP - 2941

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 13

ER -