Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl

Research output: Contribution to journalJournal articlepeer-review

Standard

Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl. / Hou, Wenya; Nemitz, Sabine; Schopper, Simone; Nielsen, Michael Lund; Kessels, Michael Manfred; Qualmann, Britta.

In: Developmental Cell, Vol. 45, No. 2, 2018, p. 262-275.E8.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Hou, W, Nemitz, S, Schopper, S, Nielsen, ML, Kessels, MM & Qualmann, B 2018, 'Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl', Developmental Cell, vol. 45, no. 2, pp. 262-275.E8. https://doi.org/10.1016/j.devcel.2018.03.007

APA

Hou, W., Nemitz, S., Schopper, S., Nielsen, M. L., Kessels, M. M., & Qualmann, B. (2018). Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl. Developmental Cell, 45(2), 262-275.E8. https://doi.org/10.1016/j.devcel.2018.03.007

Vancouver

Hou W, Nemitz S, Schopper S, Nielsen ML, Kessels MM, Qualmann B. Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl. Developmental Cell. 2018;45(2):262-275.E8. https://doi.org/10.1016/j.devcel.2018.03.007

Author

Hou, Wenya ; Nemitz, Sabine ; Schopper, Simone ; Nielsen, Michael Lund ; Kessels, Michael Manfred ; Qualmann, Britta. / Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl. In: Developmental Cell. 2018 ; Vol. 45, No. 2. pp. 262-275.E8.

Bibtex

@article{d37f5ee160e5408780b5b34049dc815f,
title = "Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl",
abstract = "The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitations, coimmunoprecipitations, cellular reconstitutions, and in vitro reconstitutions demonstrated that Cobl associates with the protein arginine methyltransferase PRMT2 in a Src Homology 3 (SH3) domain-dependent manner and that this promotes methylation of Cobl's actin nucleating C-terminal domain. Consistently, PRMT2 phenocopied Cobl functions in both gain- and loss-of-function studies. Both PRMT2- and Cobl-promoted dendritogenesis relied on methylation. PRMT2 effects require both its catalytic domain and SH3 domain. Cobl-mediated dendritic arborization required PRMT2, complex formation with PRMT2, and PRMT2's catalytic activity. Mechanistic studies reveal that Cobl methylation is key for Cobl actin binding. Therefore, arginine methylation is a regulatory mechanism reaching beyond controlling nuclear processes. It also controls a major, cytosolic, cytoskeletal component shaping neuronal cells.",
author = "Wenya Hou and Sabine Nemitz and Simone Schopper and Nielsen, {Michael Lund} and Kessels, {Michael Manfred} and Britta Qualmann",
note = "Copyright {\textcopyright} 2018 Elsevier Inc. All rights reserved.",
year = "2018",
doi = "10.1016/j.devcel.2018.03.007",
language = "English",
volume = "45",
pages = "262--275.E8",
journal = "Developmental Cell",
issn = "1534-5807",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - Arginine Methylation by PRMT2 Controls the Functions of the Actin Nucleator Cobl

AU - Hou, Wenya

AU - Nemitz, Sabine

AU - Schopper, Simone

AU - Nielsen, Michael Lund

AU - Kessels, Michael Manfred

AU - Qualmann, Britta

N1 - Copyright © 2018 Elsevier Inc. All rights reserved.

PY - 2018

Y1 - 2018

N2 - The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitations, coimmunoprecipitations, cellular reconstitutions, and in vitro reconstitutions demonstrated that Cobl associates with the protein arginine methyltransferase PRMT2 in a Src Homology 3 (SH3) domain-dependent manner and that this promotes methylation of Cobl's actin nucleating C-terminal domain. Consistently, PRMT2 phenocopied Cobl functions in both gain- and loss-of-function studies. Both PRMT2- and Cobl-promoted dendritogenesis relied on methylation. PRMT2 effects require both its catalytic domain and SH3 domain. Cobl-mediated dendritic arborization required PRMT2, complex formation with PRMT2, and PRMT2's catalytic activity. Mechanistic studies reveal that Cobl methylation is key for Cobl actin binding. Therefore, arginine methylation is a regulatory mechanism reaching beyond controlling nuclear processes. It also controls a major, cytosolic, cytoskeletal component shaping neuronal cells.

AB - The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitations, coimmunoprecipitations, cellular reconstitutions, and in vitro reconstitutions demonstrated that Cobl associates with the protein arginine methyltransferase PRMT2 in a Src Homology 3 (SH3) domain-dependent manner and that this promotes methylation of Cobl's actin nucleating C-terminal domain. Consistently, PRMT2 phenocopied Cobl functions in both gain- and loss-of-function studies. Both PRMT2- and Cobl-promoted dendritogenesis relied on methylation. PRMT2 effects require both its catalytic domain and SH3 domain. Cobl-mediated dendritic arborization required PRMT2, complex formation with PRMT2, and PRMT2's catalytic activity. Mechanistic studies reveal that Cobl methylation is key for Cobl actin binding. Therefore, arginine methylation is a regulatory mechanism reaching beyond controlling nuclear processes. It also controls a major, cytosolic, cytoskeletal component shaping neuronal cells.

U2 - 10.1016/j.devcel.2018.03.007

DO - 10.1016/j.devcel.2018.03.007

M3 - Journal article

C2 - 29689199

VL - 45

SP - 262-275.E8

JO - Developmental Cell

JF - Developmental Cell

SN - 1534-5807

IS - 2

ER -

ID: 195766906