scholarly journals The Role of Protein Arginine Methylation as Post-Translational Modification on Actin Cytoskeletal Components in Neuronal Structure and Function

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1079
Author(s):  
Britta Qualmann ◽  
Michael M. Kessels
Keyword(s):  
Actin Filament ◽  
Regulatory Mechanism ◽  
De Novo ◽  
Arginine Methylation ◽  
Loss Of Function ◽  
Filament Formation ◽  
Post Translational Modification ◽  
Neuronal Structure ◽  
Actin Nucleation ◽  
Protein Arginine Methylation

The brain encompasses a complex network of neurons with exceptionally elaborated morphologies of their axonal (signal-sending) and dendritic (signal-receiving) parts. De novo actin filament formation is one of the major driving and steering forces for the development and plasticity of the neuronal arbor. Actin filament assembly and dynamics thus require tight temporal and spatial control. Such control is particularly effective at the level of regulating actin nucleation-promoting factors, as these are key components for filament formation. Arginine methylation represents an important post-translational regulatory mechanism that had previously been mainly associated with controlling nuclear processes. We will review and discuss emerging evidence from inhibitor studies and loss-of-function models for protein arginine methyltransferases (PRMTs), both in cells and whole organisms, that unveil that protein arginine methylation mediated by PRMTs represents an important regulatory mechanism in neuritic arbor formation, as well as in dendritic spine induction, maturation and plasticity. Recent results furthermore demonstrated that arginine methylation regulates actin cytosolic cytoskeletal components not only as indirect targets through additional signaling cascades, but can also directly control an actin nucleation-promoting factor shaping neuronal cells—a key process for the formation of neuronal networks in vertebrate brains.

scholarly journals Arginine methylation helps SepIVA balance regulation of septation and elongation in Mycobacterium smegmatis

2021 ◽  
Author(s):  
Angela H Freeman ◽  
Karen Tembiwa ◽  
James R Brenner ◽  
Michael R Chase ◽  
Sarah M Fortune ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Smegmatis ◽  
Physiological Role ◽  
Arginine Methylation ◽  
Post Translational Modification ◽  
Polar Localization ◽  
Division Factor ◽  
Protein Arginine Methylation ◽  
First Time

AbstractGrowth of mycobacterial cells requires successful coordination between elongation and division of the cell wall. However, it is not clear which factors directly mediate this coordination. Here, we studied the function and post-translational modification of an essential division factor, SepIVA, in Mycobacterium smegmatis. We find that SepIVA is arginine methylated, and that these modifications alter both division and polar elongation of Msmeg. Furthermore, SepIVA impacts the localization of MurG. Polar localization of MurG correlates with polar elongation in arginine methylation mutants of sepIVA. These results establish SepIVA as a regulator of both elongation and division, and characterize a physiological role for protein arginine methylation for the first time in bacteria.

Biochemical and Computational Approaches for the Large-Scale Analysis of Protein Arginine Methylation by Mass Spectrometry

2020 ◽  
Vol 21 (7) ◽  
pp. 725-739
Author(s):  
Daniele Musiani ◽  
Enrico Massignani ◽  
Alessandro Cuomo ◽  
Avinash Yadav ◽  
Tiziana Bonaldi
Keyword(s):  
Mass Spectrometry ◽  
Large Scale ◽  
High Resolution Mass Spectrometry ◽  
Arginine Methylation ◽  
Research Field ◽  
Scale Analysis ◽  
Post Translational Modification ◽  
Large Scale Analysis ◽  
Protein Arginine Methylation

: The absence of efficient mass spectrometry-based approaches for the large-scale analysis of protein arginine methylation has hindered the understanding of its biological role, beyond the transcriptional regulation occurring through histone modification. In the last decade, however, several technological advances of both the biochemical methods for methylated polypeptide enrichment and the computational pipelines for MS data analysis have considerably boosted this research field, generating novel insights about the extent and role of this post-translational modification. : Here, we offer an overview of state-of-the-art approaches for the high-confidence identification and accurate quantification of protein arginine methylation by high-resolution mass spectrometry methods, which comprise the development of both biochemical and bioinformatics methods. The further optimization and systematic application of these analytical solutions will lead to ground-breaking discoveries on the role of protein methylation in biological processes.

scholarly journals GhVTC1, the Key Gene for Ascorbate Biosynthesis in Gossypium hirsutum, Involves in Cell Elongation Under Control of Ethylene

Cells ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 1039 ◽  
Author(s):  
Song ◽  
Wang ◽  
Chen ◽  
Ma ◽  
Zuo ◽  
...  
Keyword(s):  
Cell Growth ◽  
Gossypium Hirsutum ◽  
Cell Elongation ◽  
Regulatory Mechanism ◽  
De Novo ◽  
Primary Root ◽  
Ectopic Expression ◽  
Cellular Level ◽  
Loss Of Function ◽  
Ethylene Signaling Pathway

L-Ascorbate (Asc) plays important roles in cell growth and plant development, and its de novo biosynthesis was catalyzed by the first rate-limiting enzyme VTC1. However, the function and regulatory mechanism of VTC1 involved in cell development is obscure in Gossypium hirsutum. Herein, the Asc content and AsA/DHA ratio were accumulated and closely linked with fiber development. The GhVTC1 encoded a typical VTC1 protein with functional conserved domains and expressed preferentially during fiber fast elongation stages. Functional complementary analysis of GhVTC1 in the loss-of-function Arabidopsis vtc1-1 mutants indicated that GhVTC1 is genetically functional to rescue the defects of mutants to normal or wild type (WT). The significant shortened primary root in vtc1-1 mutants was promoted to the regular length of WT by the ectopic expression of GhVTC1 in the mutants. Additionally, GhVTC1 expression was induced by ethylene precursor 1-aminocyclopropane-1-carboxylic acid (ACC), and the GhVTC1 promoter showed high activity and included two ethylene-responsive elements (ERE). Moreover, the 5’-truncted promoters containing the ERE exhibited increased activity by ACC treatment. Our results firstly report the cotton GhVTC1 function in promoting cell elongation at the cellular level, and serve as a foundation for further understanding the regulatory mechanism of Asc-mediated cell growth via the ethylene signaling pathway.

scholarly journals Protein arginine methyltransferases: promising targets for cancer therapy

2021 ◽  
Author(s):  
Jee Won Hwang ◽  
Yena Cho ◽  
Gyu-Un Bae ◽  
Su-Nam Kim ◽  
Yong Kee Kim
Keyword(s):  
Cell Cycle ◽  
Cancer Therapy ◽  
Phase 1 ◽  
Cell Types ◽  
Arginine Methylation ◽  
Protein Methylation ◽  
Post Translational Modification ◽  
Nonhistone Proteins ◽  
Protein Arginine Methyltransferases ◽  
Protein Arginine Methylation

AbstractProtein methylation, a post-translational modification (PTM), is observed in a wide variety of cell types from prokaryotes to eukaryotes. With recent and rapid advancements in epigenetic research, the importance of protein methylation has been highlighted. The methylation of histone proteins that contributes to the epigenetic histone code is not only dynamic but is also finely controlled by histone methyltransferases and demethylases, which are essential for the transcriptional regulation of genes. In addition, many nonhistone proteins are methylated, and these modifications govern a variety of cellular functions, including RNA processing, translation, signal transduction, DNA damage response, and the cell cycle. Recently, the importance of protein arginine methylation, especially in cell cycle regulation and DNA repair processes, has been noted. Since the dysregulation of protein arginine methylation is closely associated with cancer development, protein arginine methyltransferases (PRMTs) have garnered significant interest as novel targets for anticancer drug development. Indeed, several PRMT inhibitors are in phase 1/2 clinical trials. In this review, we discuss the biological functions of PRMTs in cancer and the current development status of PRMT inhibitors in cancer therapy.

scholarly journals Parallel assembly of actin and tropomyosin, but not myosin II, during de novo actin filament formation in live mice

2018 ◽  
Vol 131 (6) ◽  
pp. jcs212654 ◽  
Author(s):  
Andrius Masedunskas ◽  
Mark A. Appaduray ◽  
Christine A. Lucas ◽  
María Lastra Cagigas ◽  
Marco Heydecker ◽  
...  
Keyword(s):  
Actin Filament ◽  
De Novo ◽  
Myosin Ii ◽  
Filament Formation ◽  
Parallel Assembly

Nebulin and N-WASP Cooperate to Cause IGF-1–Induced Sarcomeric Actin Filament Formation

Science ◽  
2010 ◽  
Vol 330 (6010) ◽  
pp. 1536-1540 ◽  
Author(s):  
Kazunori Takano ◽  
Haruko Watanabe-Takano ◽  
Shiro Suetsugu ◽  
Souichi Kurita ◽  
Kazuya Tsujita ◽  
...  
Keyword(s):  
Actin Filament ◽  
Actin Filaments ◽  
Muscle Hypertrophy ◽  
Glycogen Synthase ◽  
Akt Signaling ◽  
Glycogen Synthase Kinase 3Β ◽  
Filament Formation ◽  
Phosphatidylinositol 3 Kinase ◽  
Actin Nucleation ◽  
Signaling Mechanisms

Insulin-like growth factor 1 (IGF-1) induces skeletal muscle maturation and enlargement (hypertrophy). These responses require protein synthesis and myofibril formation (myofibrillogenesis). However, the signaling mechanisms of myofibrillogenesis remain obscure. We found that IGF-1–induced phosphatidylinositol 3-kinase–Akt signaling formed a complex of nebulin and N-WASP at the Z bands of myofibrils by interfering with glycogen synthase kinase-3β in mice. Although N-WASP is known to be an activator of the Arp2/3 complex to form branched actin filaments, the nebulin–N-WASP complex caused actin nucleation for unbranched actin filament formation from the Z bands without the Arp2/3 complex. Furthermore, N-WASP was required for IGF-1–induced muscle hypertrophy. These findings present the mechanisms of IGF-1–induced actin filament formation in myofibrillogenesis required for muscle maturation and hypertrophy and a mechanism of actin nucleation.

scholarly journals Arginine Methylation in Brain Tumors: Tumor Biology and Therapeutic Strategies

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 124
Author(s):  
Jean-Paul Bryant ◽  
John Heiss ◽  
Yeshavanth Kumar Banasavadi-Siddegowda
Keyword(s):  
Brain Tumors ◽  
Cancer Biology ◽  
Metabolic Diseases ◽  
Tumor Biology ◽  
Arginine Methylation ◽  
Post Translational Modification ◽  
Cellular Regulation ◽  
Aberrant Expression ◽  
Arginine Residues ◽  
Protein Arginine Methylation

Protein arginine methylation is a common post-translational modification that plays a pivotal role in cellular regulation. Protein arginine methyltransferases (PRMTs) catalyze the modification of target proteins by adding methyl groups to the guanidino nitrogen atoms of arginine residues. Protein arginine methylation takes part in epigenetic and cellular regulation and has been linked to neurodegenerative diseases, metabolic diseases, and tumor progression. Aberrant expression of PRMTs is associated with the development of brain tumors such as glioblastoma and medulloblastoma. Identifying PRMTs as plausible contributors to tumorigenesis has led to preclinical and clinical investigations of PRMT inhibitors for glioblastoma and medulloblastoma therapy. In this review, we discuss the role of arginine methylation in cancer biology and provide an update on the use of small molecule inhibitors of PRMTs to treat glioblastoma, medulloblastoma, and other cancers.

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