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SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis
Arginine methylation is a common posttranslational modification that modulates protein function. SCY1-like pseudokinase 1 (SCYL1) is crucial for neuronal functions and interacts with γ(2)-COP to form coat protein complex I (COPI) vesicles that regulate Golgi morphology. However, the molecular mechan...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7543066/ https://www.ncbi.nlm.nih.gov/pubmed/32583741 http://dx.doi.org/10.1091/mbc.E20-02-0100 |
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author | Amano, Genki Matsuzaki, Shinsuke Mori, Yasutake Miyoshi, Ko Han, Sarina Shikada, Sho Takamura, Hironori Yoshimura, Takeshi Katayama, Taiichi |
author_facet | Amano, Genki Matsuzaki, Shinsuke Mori, Yasutake Miyoshi, Ko Han, Sarina Shikada, Sho Takamura, Hironori Yoshimura, Takeshi Katayama, Taiichi |
author_sort | Amano, Genki |
collection | PubMed |
description | Arginine methylation is a common posttranslational modification that modulates protein function. SCY1-like pseudokinase 1 (SCYL1) is crucial for neuronal functions and interacts with γ(2)-COP to form coat protein complex I (COPI) vesicles that regulate Golgi morphology. However, the molecular mechanism by which SCYL1 is regulated remains unclear. Here, we report that the γ(2)-COP-binding site of SCYL1 is arginine-methylated by protein arginine methyltransferase 1 (PRMT1) and that SCYL1 arginine methylation is important for the interaction of SCYL1 with γ(2)-COP. PRMT1 was colocalized with SCYL1 in the Golgi fraction. Inhibition of PRMT1 suppressed axon outgrowth and dendrite complexity via abnormal Golgi morphology. Knockdown of SCYL1 by small interfering RNA (siRNA) inhibited axon outgrowth, and the inhibitory effect was rescued by siRNA-resistant SCYL1, but not SCYL1 mutant, in which the arginine methylation site was replaced. Thus, PRMT1 regulates Golgi morphogenesis via SCYL1 arginine methylation. We propose that SCYL1 arginine methylation by PRMT1 contributes to axon and dendrite morphogenesis in neurons. |
format | Online Article Text |
id | pubmed-7543066 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-75430662020-10-30 SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis Amano, Genki Matsuzaki, Shinsuke Mori, Yasutake Miyoshi, Ko Han, Sarina Shikada, Sho Takamura, Hironori Yoshimura, Takeshi Katayama, Taiichi Mol Biol Cell Articles Arginine methylation is a common posttranslational modification that modulates protein function. SCY1-like pseudokinase 1 (SCYL1) is crucial for neuronal functions and interacts with γ(2)-COP to form coat protein complex I (COPI) vesicles that regulate Golgi morphology. However, the molecular mechanism by which SCYL1 is regulated remains unclear. Here, we report that the γ(2)-COP-binding site of SCYL1 is arginine-methylated by protein arginine methyltransferase 1 (PRMT1) and that SCYL1 arginine methylation is important for the interaction of SCYL1 with γ(2)-COP. PRMT1 was colocalized with SCYL1 in the Golgi fraction. Inhibition of PRMT1 suppressed axon outgrowth and dendrite complexity via abnormal Golgi morphology. Knockdown of SCYL1 by small interfering RNA (siRNA) inhibited axon outgrowth, and the inhibitory effect was rescued by siRNA-resistant SCYL1, but not SCYL1 mutant, in which the arginine methylation site was replaced. Thus, PRMT1 regulates Golgi morphogenesis via SCYL1 arginine methylation. We propose that SCYL1 arginine methylation by PRMT1 contributes to axon and dendrite morphogenesis in neurons. The American Society for Cell Biology 2020-08-15 /pmc/articles/PMC7543066/ /pubmed/32583741 http://dx.doi.org/10.1091/mbc.E20-02-0100 Text en © 2020 Amano et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License. |
spellingShingle | Articles Amano, Genki Matsuzaki, Shinsuke Mori, Yasutake Miyoshi, Ko Han, Sarina Shikada, Sho Takamura, Hironori Yoshimura, Takeshi Katayama, Taiichi SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title | SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title_full | SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title_fullStr | SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title_full_unstemmed | SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title_short | SCYL1 arginine methylation by PRMT1 is essential for neurite outgrowth via Golgi morphogenesis |
title_sort | scyl1 arginine methylation by prmt1 is essential for neurite outgrowth via golgi morphogenesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7543066/ https://www.ncbi.nlm.nih.gov/pubmed/32583741 http://dx.doi.org/10.1091/mbc.E20-02-0100 |
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