scholarly journals New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles of Oryctolagus cuniculus

2020 ◽  
Vol 21 (21) ◽  
pp. 8319 ◽  
Author(s):  
Anna V. Glyakina ◽  
Alexey K. Surin ◽  
Sergei Yu. Grishin ◽  
Olga M. Selivanova ◽  
Mariya Yu. Suvorina ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Mass Spectrometry ◽  
Scientific Evidence ◽  
Limited Proteolysis ◽  
Mass Spectrometry Analysis ◽  
Filamentous Actin ◽  
X Ray Diffraction ◽  
Spectrometry Analysis ◽  
Actin Organization ◽  
Cellular Processes

To date, some scientific evidence (limited proteolysis, mass spectrometry analysis, electron microscopy (EM)) has accumulated, which indicates that the generally accepted model of double-stranded of filamentous actin (F-actin) organization in eukaryotic cells is not the only one. This entails an ambiguous understanding of many of the key cellular processes in which F-actin is involved. For a detailed understanding of the mechanism of F-actin assembly and actin interaction with its partners, it is necessary to take into account the polymorphism of the structural organization of F-actin at the molecular level. Using electron microscopy, limited proteolysis, mass spectrometry, X-ray diffraction, and structural modeling we demonstrated that F-actin presented in the EM images has no double-stranded organization, the regions of protease resistance are accessible for action of proteases in F-actin models. Based on all data, a new spatial model of filamentous actin is proposed, and the F-actin polymorphism is discussed.

scholarly journals PTEN arginine methylation by PRMT6 suppresses PI3K–AKT signaling and modulates pre-mRNA splicing

2019 ◽  
Vol 116 (14) ◽  
pp. 6868-6877 ◽  
Author(s):  
Jiawen Feng ◽  
Yaping Dang ◽  
Weiqi Zhang ◽  
Xuyang Zhao ◽  
Cong Zhang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Alternative Splicing ◽  
Posttranslational Modification ◽  
Arginine Methylation ◽  
Akt Signaling ◽  
Mrna Splicing ◽  
Mass Spectrometry Analysis ◽  
Arginine Methyltransferase ◽  
Spectrometry Analysis ◽  
Cellular Processes

Arginine methylation is a ubiquitous posttranslational modification that regulates critical cellular processes including signal transduction and pre-mRNA splicing. Here, we report that the tumor-suppressor PTEN is methylated by protein arginine methyltransferase 6 (PRMT6). Mass-spectrometry analysis reveals that PTEN is dimethylated at arginine 159 (R159). We found that PTEN is mutated at R159 in cancers, and the PTEN mutant R159K loses its capability to inhibit the PI3K–AKT cascade. Furthermore, PRMT6 is physically associated with PTEN, promotes asymmetrical dimethylation of PTEN, and regulates the PI3K–AKT cascade through PTEN R159 methylation. In addition, using transcriptome analyses, we found that PTEN R159 methylation is involved in modulation of pre-mRNA alternative splicing. Our results demonstrate that PTEN is functionally regulated by arginine methylation. We propose that PTEN arginine methylation modulates pre-mRNA alternative splicing and influences diverse physiologic processes.

Domain Architecture of the p62 Subunit from the Human Transcription/Repair Factor TFIIH Deduced by Limited Proteolysis and Mass Spectrometry Analysis†

Biochemistry ◽  
2004 ◽  
Vol 43 (45) ◽  
pp. 14420-14430 ◽  
Author(s):  
Anass Jawhari ◽  
Stéphanie Boussert ◽  
Valérie Lamour ◽  
R. Andrew Atkinson ◽  
Bruno Kieffer ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Domain Architecture ◽  
Limited Proteolysis ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Repair Factor

scholarly journals Effect of Ocular Hypertension on D-β-Aspartic Acid-Containing Proteins in the Retinas of Rats

2019 ◽  
Vol 2019 ◽  
pp. 1-8 ◽  
Author(s):  
Takashi Kanamoto ◽  
Takashi Tachibana ◽  
Yasushi Kitaoka ◽  
Toshio Hisatomi ◽  
Yasuhiro Ikeda ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ocular Hypertension ◽  
Aspartic Acid ◽  
Atp Synthase ◽  
Wistar Rats ◽  
Protein Band ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Spectrometry Analysis ◽  
Sds Page

Purpose. To investigate the effect of ocular hypertension-induced isomerization of aspartic acid in retinal proteins. Methods. Adult Wistar rats with ocular hypertension were used as an experimental model. D-β-aspartic acid-containing proteins were isolated by SDS-PAGE and western blot with an anti-D-β-aspartic acid antibody and identified by liquid chromatography-mass spectrometry analysis. The concentration of ATP was measured by ELISA. Results. D-β-aspartic acid was expressed in a protein band at around 44.5 kDa at much higher quantities in the retinas of rats with ocular hypertension than in those of normotensive rats. The 44.5 kDa protein band was mainly composed of α-enolase, S-arrestin, and ATP synthase subunits α and β, in both the ocular hypertensive and normotensive retinas. Moreover, increasing intraocular pressure was correlated with increasing ATP concentrations in the retinas of rats. Conclusion. Ocular hypertension affected the expression of proteins containing D-β-aspartic acid, including ATP synthase subunits, and up-regulation of ATP in the retinas of rats.

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