Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2

Research output: Contribution to journalJournal article

Standard

Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2. / Trulley, Philipp; Snieckute, Goda; Bekker-Jensen, Dorte; Menon, Manoj B; Freund, Robert; Kotlyarov, Alexey; Olsen, Jesper V; Diaz-Muñoz, Manuel D; Turner, Martin; Bekker-Jensen, Simon; Gaestel, Matthias; Tiedje, Christopher.

In: Cell Reports, Vol. 27, No. 10, 2019, p. 2859-2870.e6.

Research output: Contribution to journalJournal article

Harvard

Trulley, P, Snieckute, G, Bekker-Jensen, D, Menon, MB, Freund, R, Kotlyarov, A, Olsen, JV, Diaz-Muñoz, MD, Turner, M, Bekker-Jensen, S, Gaestel, M & Tiedje, C 2019, 'Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2', Cell Reports, vol. 27, no. 10, pp. 2859-2870.e6. https://doi.org/10.1016/j.celrep.2019.05.024

APA

Trulley, P., Snieckute, G., Bekker-Jensen, D., Menon, M. B., Freund, R., Kotlyarov, A., ... Tiedje, C. (2019). Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2. Cell Reports, 27(10), 2859-2870.e6. https://doi.org/10.1016/j.celrep.2019.05.024

Vancouver

Trulley P, Snieckute G, Bekker-Jensen D, Menon MB, Freund R, Kotlyarov A et al. Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2. Cell Reports. 2019;27(10):2859-2870.e6. https://doi.org/10.1016/j.celrep.2019.05.024

Author

Trulley, Philipp ; Snieckute, Goda ; Bekker-Jensen, Dorte ; Menon, Manoj B ; Freund, Robert ; Kotlyarov, Alexey ; Olsen, Jesper V ; Diaz-Muñoz, Manuel D ; Turner, Martin ; Bekker-Jensen, Simon ; Gaestel, Matthias ; Tiedje, Christopher. / Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2. In: Cell Reports. 2019 ; Vol. 27, No. 10. pp. 2859-2870.e6.

Bibtex

@article{817ed9f440a94802b7c5455d8600f92d,
title = "Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2",
abstract = "Alternative translation is an important mechanism of post-transcriptional gene regulation leading to the expression of different protein isoforms originating from the same mRNA. Here, we describe an abundant long isoform of the stress/p38MAPK-activated protein kinase MK2. This isoform is constitutively translated from an alternative CUG translation initiation start site located in the 5' UTR of its mRNA. The RNA helicase eIF4A1 is needed to ensure translation of the long and the known short isoforms of MK2, of which the molecular properties were determined. Only the short isoform phosphorylated Hsp27 in vivo, supported migration and stress-induced immediate early gene (IEG) expression. Interaction profiling revealed short-isoform-specific binding partners that were associated with migration. In contrast, the long isoform contains at least one additional phosphorylatable serine in its unique N terminus. In sum, our data reveal a longer isoform of MK2 with distinct physiological properties.",
author = "Philipp Trulley and Goda Snieckute and Dorte Bekker-Jensen and Menon, {Manoj B} and Robert Freund and Alexey Kotlyarov and Olsen, {Jesper V} and Diaz-Mu{\~n}oz, {Manuel D} and Martin Turner and Simon Bekker-Jensen and Matthias Gaestel and Christopher Tiedje",
year = "2019",
doi = "10.1016/j.celrep.2019.05.024",
language = "English",
volume = "27",
pages = "2859--2870.e6",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "10",

}

RIS

TY - JOUR

T1 - Alternative Translation Initiation Generates a Functionally Distinct Isoform of the Stress-Activated Protein Kinase MK2

AU - Trulley, Philipp

AU - Snieckute, Goda

AU - Bekker-Jensen, Dorte

AU - Menon, Manoj B

AU - Freund, Robert

AU - Kotlyarov, Alexey

AU - Olsen, Jesper V

AU - Diaz-Muñoz, Manuel D

AU - Turner, Martin

AU - Bekker-Jensen, Simon

AU - Gaestel, Matthias

AU - Tiedje, Christopher

PY - 2019

Y1 - 2019

N2 - Alternative translation is an important mechanism of post-transcriptional gene regulation leading to the expression of different protein isoforms originating from the same mRNA. Here, we describe an abundant long isoform of the stress/p38MAPK-activated protein kinase MK2. This isoform is constitutively translated from an alternative CUG translation initiation start site located in the 5' UTR of its mRNA. The RNA helicase eIF4A1 is needed to ensure translation of the long and the known short isoforms of MK2, of which the molecular properties were determined. Only the short isoform phosphorylated Hsp27 in vivo, supported migration and stress-induced immediate early gene (IEG) expression. Interaction profiling revealed short-isoform-specific binding partners that were associated with migration. In contrast, the long isoform contains at least one additional phosphorylatable serine in its unique N terminus. In sum, our data reveal a longer isoform of MK2 with distinct physiological properties.

AB - Alternative translation is an important mechanism of post-transcriptional gene regulation leading to the expression of different protein isoforms originating from the same mRNA. Here, we describe an abundant long isoform of the stress/p38MAPK-activated protein kinase MK2. This isoform is constitutively translated from an alternative CUG translation initiation start site located in the 5' UTR of its mRNA. The RNA helicase eIF4A1 is needed to ensure translation of the long and the known short isoforms of MK2, of which the molecular properties were determined. Only the short isoform phosphorylated Hsp27 in vivo, supported migration and stress-induced immediate early gene (IEG) expression. Interaction profiling revealed short-isoform-specific binding partners that were associated with migration. In contrast, the long isoform contains at least one additional phosphorylatable serine in its unique N terminus. In sum, our data reveal a longer isoform of MK2 with distinct physiological properties.

U2 - 10.1016/j.celrep.2019.05.024

DO - 10.1016/j.celrep.2019.05.024

M3 - Journal article

C2 - 31167133

VL - 27

SP - 2859-2870.e6

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 10

ER -

ID: 222692099