PRMT5-mediated regulatory arginine methylation of RIPK3

Research output: Contribution to journal › Journal article › Research › peer-review

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PRMT5-mediated regulatory arginine methylation of RIPK3. / Chauhan, Chanchal; Martinez-Val, Ana; Niedenthal, Rainer; Olsen, Jesper Velgaard; Kotlyarov, Alexey; Bekker-Jensen, Simon; Gaestel, Matthias; Menon, Manoj B.

In: Cell Death Discovery, Vol. 9, 14, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Chauhan, C, Martinez-Val, A, Niedenthal, R, Olsen, JV, Kotlyarov, A, Bekker-Jensen, S, Gaestel, M & Menon, MB 2023, 'PRMT5-mediated regulatory arginine methylation of RIPK3', Cell Death Discovery, vol. 9, 14. https://doi.org/10.1038/s41420-023-01299-z

APA

Chauhan, C., Martinez-Val, A., Niedenthal, R., Olsen, J. V., Kotlyarov, A., Bekker-Jensen, S., Gaestel, M., & Menon, M. B. (2023). PRMT5-mediated regulatory arginine methylation of RIPK3. Cell Death Discovery, 9, [14]. https://doi.org/10.1038/s41420-023-01299-z

Vancouver

Chauhan C, Martinez-Val A, Niedenthal R, Olsen JV, Kotlyarov A, Bekker-Jensen S et al. PRMT5-mediated regulatory arginine methylation of RIPK3. Cell Death Discovery. 2023;9. 14. https://doi.org/10.1038/s41420-023-01299-z

Author

Chauhan, Chanchal ; Martinez-Val, Ana ; Niedenthal, Rainer ; Olsen, Jesper Velgaard ; Kotlyarov, Alexey ; Bekker-Jensen, Simon ; Gaestel, Matthias ; Menon, Manoj B. / PRMT5-mediated regulatory arginine methylation of RIPK3. In: Cell Death Discovery. 2023 ; Vol. 9.

Bibtex

@article{ad3515a7feaa465d87fbed8d4c9232a1,
title = "PRMT5-mediated regulatory arginine methylation of RIPK3",
abstract = "The TNF receptor-interacting protein kinases (RIPK)-1 and 3 are regulators of extrinsic cell death response pathways, where RIPK1 makes the cell survival or death decisions by associating with distinct complexes mediating survival signaling, caspase activation or RIPK3-dependent necroptotic cell death in a context-dependent manner. Using a mass spectrometry-based screen to find new components of the ripoptosome/necrosome, we discovered the protein-arginine methyltransferase (PRMT)-5 as a direct interaction partner of RIPK1. Interestingly, RIPK3 but not RIPK1 was then found to be a target of PRMT5-mediated symmetric arginine dimethylation. A conserved arginine residue in RIPK3 (R486 in human, R415 in mouse) was identified as the evolutionarily conserved target for PRMT5-mediated symmetric dimethylation and the mutations R486A and R486K in human RIPK3 almost completely abrogated its methylation. Rescue experiments using these non-methylatable mutants of RIPK3 demonstrated PRMT5-mediated RIPK3 methylation to act as an efficient mechanism of RIPK3-mediated feedback control on RIPK1 activity and function. Therefore, this study reveals PRMT5-mediated RIPK3 methylation as a novel modulator of RIPK1-dependent signaling.",
author = "Chanchal Chauhan and Ana Martinez-Val and Rainer Niedenthal and Olsen, {Jesper Velgaard} and Alexey Kotlyarov and Simon Bekker-Jensen and Matthias Gaestel and Menon, {Manoj B}",
note = "{\textcopyright} 2023. The Author(s).",
year = "2023",
doi = "10.1038/s41420-023-01299-z",
language = "English",
volume = "9",
journal = "Cell Death Discovery",
issn = "2058-7716",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - PRMT5-mediated regulatory arginine methylation of RIPK3

AU - Chauhan, Chanchal

AU - Martinez-Val, Ana

AU - Niedenthal, Rainer

AU - Olsen, Jesper Velgaard

AU - Kotlyarov, Alexey

AU - Bekker-Jensen, Simon

AU - Gaestel, Matthias

AU - Menon, Manoj B

N1 - © 2023. The Author(s).

PY - 2023

Y1 - 2023

N2 - The TNF receptor-interacting protein kinases (RIPK)-1 and 3 are regulators of extrinsic cell death response pathways, where RIPK1 makes the cell survival or death decisions by associating with distinct complexes mediating survival signaling, caspase activation or RIPK3-dependent necroptotic cell death in a context-dependent manner. Using a mass spectrometry-based screen to find new components of the ripoptosome/necrosome, we discovered the protein-arginine methyltransferase (PRMT)-5 as a direct interaction partner of RIPK1. Interestingly, RIPK3 but not RIPK1 was then found to be a target of PRMT5-mediated symmetric arginine dimethylation. A conserved arginine residue in RIPK3 (R486 in human, R415 in mouse) was identified as the evolutionarily conserved target for PRMT5-mediated symmetric dimethylation and the mutations R486A and R486K in human RIPK3 almost completely abrogated its methylation. Rescue experiments using these non-methylatable mutants of RIPK3 demonstrated PRMT5-mediated RIPK3 methylation to act as an efficient mechanism of RIPK3-mediated feedback control on RIPK1 activity and function. Therefore, this study reveals PRMT5-mediated RIPK3 methylation as a novel modulator of RIPK1-dependent signaling.

AB - The TNF receptor-interacting protein kinases (RIPK)-1 and 3 are regulators of extrinsic cell death response pathways, where RIPK1 makes the cell survival or death decisions by associating with distinct complexes mediating survival signaling, caspase activation or RIPK3-dependent necroptotic cell death in a context-dependent manner. Using a mass spectrometry-based screen to find new components of the ripoptosome/necrosome, we discovered the protein-arginine methyltransferase (PRMT)-5 as a direct interaction partner of RIPK1. Interestingly, RIPK3 but not RIPK1 was then found to be a target of PRMT5-mediated symmetric arginine dimethylation. A conserved arginine residue in RIPK3 (R486 in human, R415 in mouse) was identified as the evolutionarily conserved target for PRMT5-mediated symmetric dimethylation and the mutations R486A and R486K in human RIPK3 almost completely abrogated its methylation. Rescue experiments using these non-methylatable mutants of RIPK3 demonstrated PRMT5-mediated RIPK3 methylation to act as an efficient mechanism of RIPK3-mediated feedback control on RIPK1 activity and function. Therefore, this study reveals PRMT5-mediated RIPK3 methylation as a novel modulator of RIPK1-dependent signaling.

U2 - 10.1038/s41420-023-01299-z

DO - 10.1038/s41420-023-01299-z

M3 - Journal article

C2 - 36658119

VL - 9

JO - Cell Death Discovery

JF - Cell Death Discovery

SN - 2058-7716

M1 - 14

ER -

ID: 333470327