ArticleArchaea (Vancouver, B.C.)2010
Phosphorylation and methylation of proteasomal proteins of the haloarcheon Haloferax volcanii.
Article in Archaea (Vancouver, B.C.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- C(P)XCG Proteins ofInternational journal of molecular sciences · 2024Article
- Article
- Expression and tandem affinity purification of 20S proteasomes and other multisubunit complexes in Haloferax volcanii.Methods in enzymology · 2021Article
- Post-Translational Modifications Aid Archaeal Survival.Biomolecules · 2020Review
- The Rio1 protein kinases/ATPases: conserved regulators of growth, division, and genomic stability.Current genetics · 2019Review
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.Nature communications · 2018Article
- Insights into the evolutionary conserved regulation of Rio ATPase activity.Nucleic acids research · 2018Article
- Autophosphorylation and Cross-Phosphorylation of Protein Kinases from the CrenarchaeonFrontiers in microbiology · 2017Article
- Protein phosphorylation and its role in archaeal signal transduction.FEMS microbiology reviews · 2016Review
- Article
- Phosphorylation regulates mycobacterial proteasome.Journal of microbiology (Seoul, Korea) · 2014Article
- Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond.Journal of molecular and cellular cardiology · 2014Review
- The ancient microbial RIO kinases.The Journal of biological chemistry · 2014Review
- Protein Ser/Thr/Tyr phosphorylation in the Archaea.The Journal of biological chemistry · 2014Review
- Structural and biochemical properties of an extreme 'salt-loving' proteasome activating nucleotidase from the archaeon Haloferax volcanii.Extremophiles : life under extreme conditions · 2014Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- Prokaryotic proteasomes: nanocompartments of degradation.Journal of molecular microbiology and biotechnology · 2013Review
- Archaeal proteasomes and sampylation.Sub-cellular biochemistry · 2013Review
- Extreme challenges and advances in archaeal proteomics.Current opinion in microbiology · 2012Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Proteasomes are composed of 20S core particles (CPs) of alpha- and beta-type subunits that associate with regulatory particle AAA ATPases such as the proteasome-activating nucleotidase (PAN) complexes of archaea. In this study, the roles and additional sites of post-translational modification of proteasomes were investigated using the archaeon Haloferax volcanii as a model. Indicative of phosphorylation, phosphatase-sensitive isoforms of alpha1 and alpha2 were detected by 2-DE immunoblot. To map these and other potential sites of post-translational modification, proteasomes were purified and analyzed by tandem mass spectrometry (MS/MS). Using this approach, several phosphosites were mapped including alpha1 Thr147, alpha2 Thr13/Ser14 and PAN-A Ser340. Multiple methylation sites were also mapped to alpha1, thus, revealing a new type of proteasomal modification. Probing the biological role of alpha1 and PAN-A phosphorylation by site-directed mutagenesis revealed dominant negative phenotypes for cell viability and/or pigmentation for alpha1 variants including Thr147Ala, Thr158Ala and Ser58Ala. An H. volcanii Rio1p Ser/Thr kinase homolog was purified and shown to catalyze autophosphorylation and phosphotransfer to alpha1. The alpha1 variants in Thr and Ser residues that displayed dominant negative phenotypes were significantly reduced in their ability to accept phosphoryl groups from Rio1p, thus, providing an important link between cell physiology and proteasomal phosphorylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.