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Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2. / Wiemhoefer, Anne; Stargardt, Anita; van der Linden, Wouter A; Renner, Maria C; van Kesteren, Ronald E; Stap, Jan; Raspe, Marcel A; Tomkinson, Birgitta; Kessels, Helmut W; Ovaa, Huib; Overkleeft, Herman S; Florea, Bogdan; Reits, Eric A.

In: Molecular and Cellular Proteomics, Vol. 14, No. 8, 08.2015, p. 2177-93.

Research output: Contribution to journal/periodicalArticleScientificpeer-review

Harvard

Wiemhoefer, A, Stargardt, A, van der Linden, WA, Renner, MC, van Kesteren, RE, Stap, J, Raspe, MA, Tomkinson, B, Kessels, HW, Ovaa, H, Overkleeft, HS, Florea, B & Reits, EA 2015, 'Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2' Molecular and Cellular Proteomics, vol. 14, no. 8, pp. 2177-93. https://doi.org/10.1074/mcp.M114.043331

APA

Wiemhoefer, A., Stargardt, A., van der Linden, W. A., Renner, M. C., van Kesteren, R. E., Stap, J., ... Reits, E. A. (2015). Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2. Molecular and Cellular Proteomics, 14(8), 2177-93. https://doi.org/10.1074/mcp.M114.043331

Vancouver

Wiemhoefer A, Stargardt A, van der Linden WA, Renner MC, van Kesteren RE, Stap J et al. Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2. Molecular and Cellular Proteomics. 2015 Aug;14(8):2177-93. https://doi.org/10.1074/mcp.M114.043331

Author

Wiemhoefer, Anne ; Stargardt, Anita ; van der Linden, Wouter A ; Renner, Maria C ; van Kesteren, Ronald E ; Stap, Jan ; Raspe, Marcel A ; Tomkinson, Birgitta ; Kessels, Helmut W ; Ovaa, Huib ; Overkleeft, Herman S ; Florea, Bogdan ; Reits, Eric A. / Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2. In: Molecular and Cellular Proteomics. 2015 ; Vol. 14, No. 8. pp. 2177-93.

BibTeX

@article{444923d6c80749e2985c63956f11c674,
title = "Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2",
abstract = "Tripeptidyl peptidase II (TPP2) is a serine peptidase involved in various biological processes, including antigen processing, cell growth, DNA repair, and neuropeptide mediated signaling. The underlying mechanisms of how a peptidase can influence this multitude of processes still remain unknown. We identified rapid proteomic changes in neuroblastoma cells following selective TPP2 inhibition using the known reversible inhibitor butabindide, as well as a new, more potent, and irreversible peptide phosphonate inhibitor. Our data show that TPP2 inhibition indirectly but rapidly decreases the levels of active, di-phosphorylated extracellular signal-regulated kinase 1 (ERK1) and ERK2 in the nucleus, thereby down-regulating signal transduction downstream of growth factors and mitogenic stimuli. We conclude that TPP2 mediates many important cellular functions by controlling ERK1 and ERK2 phosphorylation. For instance, we show that TPP2 inhibition of neurons in the hippocampus leads to an excessive strengthening of synapses, indicating that TPP2 activity is crucial for normal brain function.",
author = "Anne Wiemhoefer and Anita Stargardt and {van der Linden}, {Wouter A} and Renner, {Maria C} and {van Kesteren}, {Ronald E} and Jan Stap and Raspe, {Marcel A} and Birgitta Tomkinson and Kessels, {Helmut W} and Huib Ovaa and Overkleeft, {Herman S} and Bogdan Florea and Reits, {Eric A}",
note = "{\circledC} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",
year = "2015",
month = "8",
doi = "10.1074/mcp.M114.043331",
language = "English",
volume = "14",
pages = "2177--93",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "8",

}

RIS

TY - JOUR

T1 - Tripeptidyl Peptidase II Mediates Levels of Nuclear Phosphorylated ERK1 and ERK2

AU - Wiemhoefer, Anne

AU - Stargardt, Anita

AU - van der Linden, Wouter A

AU - Renner, Maria C

AU - van Kesteren, Ronald E

AU - Stap, Jan

AU - Raspe, Marcel A

AU - Tomkinson, Birgitta

AU - Kessels, Helmut W

AU - Ovaa, Huib

AU - Overkleeft, Herman S

AU - Florea, Bogdan

AU - Reits, Eric A

N1 - © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

PY - 2015/8

Y1 - 2015/8

N2 - Tripeptidyl peptidase II (TPP2) is a serine peptidase involved in various biological processes, including antigen processing, cell growth, DNA repair, and neuropeptide mediated signaling. The underlying mechanisms of how a peptidase can influence this multitude of processes still remain unknown. We identified rapid proteomic changes in neuroblastoma cells following selective TPP2 inhibition using the known reversible inhibitor butabindide, as well as a new, more potent, and irreversible peptide phosphonate inhibitor. Our data show that TPP2 inhibition indirectly but rapidly decreases the levels of active, di-phosphorylated extracellular signal-regulated kinase 1 (ERK1) and ERK2 in the nucleus, thereby down-regulating signal transduction downstream of growth factors and mitogenic stimuli. We conclude that TPP2 mediates many important cellular functions by controlling ERK1 and ERK2 phosphorylation. For instance, we show that TPP2 inhibition of neurons in the hippocampus leads to an excessive strengthening of synapses, indicating that TPP2 activity is crucial for normal brain function.

AB - Tripeptidyl peptidase II (TPP2) is a serine peptidase involved in various biological processes, including antigen processing, cell growth, DNA repair, and neuropeptide mediated signaling. The underlying mechanisms of how a peptidase can influence this multitude of processes still remain unknown. We identified rapid proteomic changes in neuroblastoma cells following selective TPP2 inhibition using the known reversible inhibitor butabindide, as well as a new, more potent, and irreversible peptide phosphonate inhibitor. Our data show that TPP2 inhibition indirectly but rapidly decreases the levels of active, di-phosphorylated extracellular signal-regulated kinase 1 (ERK1) and ERK2 in the nucleus, thereby down-regulating signal transduction downstream of growth factors and mitogenic stimuli. We conclude that TPP2 mediates many important cellular functions by controlling ERK1 and ERK2 phosphorylation. For instance, we show that TPP2 inhibition of neurons in the hippocampus leads to an excessive strengthening of synapses, indicating that TPP2 activity is crucial for normal brain function.

U2 - 10.1074/mcp.M114.043331

DO - 10.1074/mcp.M114.043331

M3 - Article

VL - 14

SP - 2177

EP - 2193

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

SN - 1535-9476

IS - 8

ER -

ID: 1446312