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Different roles of gamma- and beta-actin in neuronal functions

ABSTRACT: Lack of cytoplasmic beta-actin gene (Actb) leads to early embryonic lethality in mice, however targeted editing of Actb coding sequence by introducing five point mutations to encode cytoplasmic gamma-actin protein does not affect mouse viability. These mice with beta to gamma actin replacement (Actbc-g mice) develop normally and show no detectable phenotypes at young age, despite complete lack of beta-actin protein. Here we investigated the effect of the replacement of beta-actin with gamma-actin in the brain and the retina --- the tissue where these two cytoplasmic actin isoforms predominate.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Dawei Dong

LAB HEAD: Dawei W Dong

PROVIDER: PXD031462 | Pride | 2023-03-11

REPOSITORIES: Pride

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	KashinaA-19-G120-Sample1-QEP.raw	Raw
	KashinaA-19-G120-Sample10-QEP.raw	Raw
	KashinaA-19-G120-Sample11-QEP.raw	Raw
	KashinaA-19-G120-Sample12-QEP.raw	Raw
	KashinaA-19-G120-Sample13-QEP.raw	Raw

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Publications

Differential N-terminal processing of beta and gamma actin.

Chen Li L Vedula Pavan P Tang Hsin Yao HY Dong Dawei W DW Kashina Anna S AS

iScience 20220923 10

Cytoplasmic beta- and gamma-actin are ubiquitously expressed in every eukaryotic cell. They are encoded by different genes, but their amino acid sequences differ only by four conservative substitutions at the N-termini, making it difficult to dissect their individual regulation. Here, we analyzed actin from cultured cells and tissues by mass spectrometry and found that beta, unlike gamma actin, undergoes sequential removal of N-terminal Asp residues, leading to truncated actin species found in b ...[more]

PMID: 36248738

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Different roles of gamma- and beta-actin in the retina

Project description:Lack of cytoplasmic beta-actin gene (Actb) leads to early embryonic lethality in mice, however targeted editing of Actb coding sequence by introducing five point mutations to encode cytoplasmic gamma-actin protein does not affect mouse viability. These mice with beta to gamma actin replacement (Actbc-g mice) develop normally and show no detectable phenotypes at young age, despite complete lack of beta-actin protein. Here we investigated the effect of the replacement of beta-actin with gamma-actin in the retina.

2023-03-11 | PXD031465 | Pride

Actb knockout in primary mouse embryonic fibroblasts LC-MS/MS

Project description:The cytoplasmic actin proteins, beta- and gamma-actin, are 99% identical but perform non-redundant functions. Genes encoding the cytoplasmic actins, Actb and Actg1, respectively, are less similar but still share 89% of their nucleotide sequences. Knockout (KO) of Actb by deletion of first coding exons 2 and 3 in mice is embryonic lethal while KO embryonic fibroblasts (MEFs) fail to proliferate. In contrast, KO of Actg1 is viable but mice lacking Actg1 present with increased perinatal lethality and Actg1 KO MEFs present with a much milder defect in cell proliferation. Recent studies have identified important protein-independent functions for both Actb and Actg1 and demonstrate that deletions within the Actb nucleotide sequence, and not loss of the beta-actin protein, cause the most severe phenotypes in KO mice and cells. Here, we use a multi-omics approach to better understand what drives the phenotypes of Actb KO MEFs. RNA-sequencing and mass spectrometry of Actb KO MEFs reveal largescale changes to the transcriptome, proteome, and phosphoproteome. Pathway analysis of genes and proteins differentially expressed upon Actb KO shows widespread dysregulation of genes involved in the cell cycle. Together, these data suggest novel, protein-independent roles for Actb in regulating gene expression associated with control of cell proliferation.

2024-02-19 | PXD039786 | Pride

N-terminal processing of beta and gamma actin in MEF cells

Project description:Actin is one of the most essential and abundant intracellular proteins, playing an essential physiological role as the major constituent of the actin cytoskeleton. Two cytoplasmic actins, beta- and gamma-actin, are encoded by different genes, but their amino acid sequences differ only by four conservative substitutions at the N-terminus, making it very difficult to dissect their individual regulation in vivo. The majority of actins are N-terminally acetylated, following the removal of N-terminal Met. Here, we analyzed beta and gamma cytoplasmic actin N-termini in different actin preparations.

2023-03-11 | PXD032139 | Pride

N-terminal processing of beta and gamma actin in human platelets

2023-03-11 | PXD032086 | Pride

N-terminal processing of beta and gamma actin in HAP1 cells

2023-03-11 | PXD031481 | Pride

Purification of Human β and γ Actin from Budding Yeast

Project description:To facilitate biochemical studies of human cytoplasmic actins, Saccharomyces cerevisiaestrains were developed that express either human β-actin or γ-actin as their sole actin. Actins purified from these strains have biochemical properties similar to mammalian skeletal muscle α-actin, but display differential binding to some key actin regulators. Mass-spectrometry analysis shows that the human actins made from yeast generally retain their N-terminal methionines, which are modified by acetylation.

2023-04-24 | PXD040174 | Pride

ChIP-Seq of H3K27ac in Actb-/- MEFs expressing NLS-tagged beta-actin

Project description:ChIP-Seq of H3K27ac in Actb-/- MEFs expressing NLS-tagged beta-actin

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Actin R256 mono-methylation is a conserved post-translational modification involved in transcription

Project description:Nuclear actin has been elusive due to the lack of molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions, and cause diseases in human. Interestingly, we show that an antibody specific for actin R256me1 preferentially stain nuclear actin over cytoplasmic actin in yeast, mouse and human cells. We also show that actin R256me1 is regulated by protein arginine methyl transferase-5 (PRMT5) in HEK293 cells. Genome-wide survey of actin R256me1 mark provides a landscape for nuclear actin correlated with transcription. Further gene expression and protein interaction studies uncover extensive correlations between actin R256me1 and active transcription. The discovery of actin R256me1 mark suggests a fundamental mechanism to distinguish nuclear actin from cytoplasmic actin through post-translational modification (PTM), and potentially implicates an actin PTM mark in transcription and human diseases.

2020-08-26 | GSE156817 | GEO

An antibody independent verification method quantifies m6A in the chicken β-actin zipcode

Project description:N6-Methyladenosine (m6A) in mRNA regulates almost every stage in the mRNA life cycle, and the development of the high throughput detection of methylated sites in mRNA using MeRIPSeq or miCLIP revolutionized the m6A research field. Both methods are based on immunoprecipitation of fragmented mRNA. However, it is well documented that antibodies often have nonspecific activities, thus verification of identified m6A sites using an antibody-independent method would be highly desirable. Currently such approaches are limited. Here we present RedBaron, an improved biochemical method for the site-specific detection and quantification of m6A in RNA. We demonstrate that the RedBaron method is able to accurately quantify m6A levels at specific transcripts in vivo. We used this assay for the site-specific detection and quantification of m6A within the chicken β-actin (ACTB) zipcode sequence in chicken embryos and in fibroblast cells. We demonstrate that methylation of this site in the β-actin zipcode enhances ZBP1 binding in vitro, whilst methylation of a nearby adenosine abolishes

2023-05-24 | GSE185078 | GEO

Sequencing analysis of beta-actin KO MEFs expressing NLS-beta-actin

Project description:Sequencing analysis of beta-actin KO MEFs expressing NLS-beta-actin

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