Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G2/M

Anna Lena Illert; Michael Zech; Cathrin Moll; Corinna Albers; Stefanie Kreutmair; Christian Peschel; Florian Bassermann; Justus Duyster

doi:10.1074/jbc.M112.373464

Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M

Anna Lena Illert
, Michael Zech
, Cathrin Moll
, Corinna Albers
, Stefanie Kreutmair
, Christian Peschel
, Florian Bassermann
, Justus Duyster

Technical University of Munich
Albert-Ludwigs-Universität Freiburg

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

12 Scopus citations

Abstract

Background: NIPA is involved in timing mitotic entry and is inactivated by phosphorylation. The kinase responsible for NIPA phosphorylation at G ₂/M is unknown. Results: We show that cell cycle-dependent phosphorylation of NIPA is mediated by ERK2. Conclusion: NIPA is identified as one of the very few ERK2-specific substrates at the G₂/M transition. Significance: This demonstrates divergent functions of ERK1 and ERK2 in cell cycle regulation.

Original language	English
Pages (from-to)	37997-38005
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	287
Issue number	45
DOIs	https://doi.org/10.1074/jbc.M112.373464
State	Published - 2 Nov 2012

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10.1074/jbc.M112.373464

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Illert, A. L., Zech, M., Moll, C., Albers, C., Kreutmair, S., Peschel, C., Bassermann, F., & Duyster, J. (2012). Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M. Journal of Biological Chemistry, 287(45), 37997-38005. https://doi.org/10.1074/jbc.M112.373464

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title = "Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G2/M",

abstract = "Background: NIPA is involved in timing mitotic entry and is inactivated by phosphorylation. The kinase responsible for NIPA phosphorylation at G 2/M is unknown. Results: We show that cell cycle-dependent phosphorylation of NIPA is mediated by ERK2. Conclusion: NIPA is identified as one of the very few ERK2-specific substrates at the G2/M transition. Significance: This demonstrates divergent functions of ERK1 and ERK2 in cell cycle regulation.",

author = "Illert, \{Anna Lena\} and Michael Zech and Cathrin Moll and Corinna Albers and Stefanie Kreutmair and Christian Peschel and Florian Bassermann and Justus Duyster",

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Illert, AL, Zech, M, Moll, C, Albers, C, Kreutmair, S, Peschel, C , Bassermann, F & Duyster, J 2012, 'Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M', Journal of Biological Chemistry, vol. 287, no. 45, pp. 37997-38005. https://doi.org/10.1074/jbc.M112.373464

Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M. / Illert, Anna Lena; Zech, Michael; Moll, Cathrin et al.
In: Journal of Biological Chemistry, Vol. 287, No. 45, 02.11.2012, p. 37997-38005.

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

TY - JOUR

T1 - Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G2/M

AU - Illert, Anna Lena

AU - Zech, Michael

AU - Moll, Cathrin

AU - Albers, Corinna

AU - Kreutmair, Stefanie

AU - Peschel, Christian

AU - Bassermann, Florian

AU - Duyster, Justus

PY - 2012/11/2

Y1 - 2012/11/2

N2 - Background: NIPA is involved in timing mitotic entry and is inactivated by phosphorylation. The kinase responsible for NIPA phosphorylation at G 2/M is unknown. Results: We show that cell cycle-dependent phosphorylation of NIPA is mediated by ERK2. Conclusion: NIPA is identified as one of the very few ERK2-specific substrates at the G2/M transition. Significance: This demonstrates divergent functions of ERK1 and ERK2 in cell cycle regulation.

AB - Background: NIPA is involved in timing mitotic entry and is inactivated by phosphorylation. The kinase responsible for NIPA phosphorylation at G 2/M is unknown. Results: We show that cell cycle-dependent phosphorylation of NIPA is mediated by ERK2. Conclusion: NIPA is identified as one of the very few ERK2-specific substrates at the G2/M transition. Significance: This demonstrates divergent functions of ERK1 and ERK2 in cell cycle regulation.

UR - https://www.scopus.com/pages/publications/84868314587

U2 - 10.1074/jbc.M112.373464

DO - 10.1074/jbc.M112.373464

M3 - Article

C2 - 22955283

AN - SCOPUS:84868314587

SN - 0021-9258

VL - 287

SP - 37997

EP - 38005

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 45

ER -

Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M

Abstract

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