Identifying ubiquitinated proteins and aggregates

Basisty, Nathan; Schilling, Birgit; Rabinovitch, Peter S.

doi:10.18632/aging.101605

Cited by 5 publications

(2 citation statements)

References 5 publications

(12 reference statements)

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“…[57] LLP populations also tend to be enriched with PTMs such as ubiquitination, oxidation, crosslinking, and carbamylation, which are sometimes used alone or in combination with other fractionation strategies to identify and quantify LLPs. [13,[58][59][60]…”

Section: Protein Turnover Measurements Using Comprehensive Proteomicsmentioning

confidence: 99%

“…Components of the ECM also tend to be long‐lived, and workflows to effectively prepare ECM protein fractions for MS have been developed . LLP populations also tend to be enriched with PTMs such as ubiquitination, oxidation, crosslinking, and carbamylation, which are sometimes used alone or in combination with other fractionation strategies to identify and quantify LLPs …”

Section: Protein Turnover Measurements Using Comprehensive Proteomicsmentioning

confidence: 99%

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Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity

2020

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Aging and age‐related diseases are accompanied by proteome remodeling and progressive declines in cellular machinery required to maintain protein homeostasis (proteostasis), such as autophagy, ubiquitin‐mediated degradation, and protein synthesis. While many studies have focused on capturing changes in proteostasis, the identification of proteins that evade these cellular processes has recently emerged as an approach to studying the aging proteome. With advances in proteomic technology, it is possible to monitor protein half‐lives and protein turnover at the level of individual proteins in vivo. For large‐scale studies, these technologies typically include the use of stable isotope labeling coupled with MS and comprehensive assessment of protein turnover rates. Protein turnover studies have revealed groups of highly relevant long‐lived proteins (LLPs), such as the nuclear pore complexes, extracellular matrix proteins, and protein aggregates. Here, the role of LLPs during aging and age‐related diseases and the methods used to identify and quantify their changes are reviewed. The methods available to conduct studies of protein turnover, used in combination with traditional proteomic methods, will enable the field to perform studies in a systems biology context, as changes in proteostasis may not be revealed in studies that solely measure differential protein abundances.

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Section: Protein Turnover Measurements Using Comprehensive Proteomicsmentioning

confidence: 99%

Section: Protein Turnover Measurements Using Comprehensive Proteomicsmentioning

confidence: 99%

Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity

2020

Self Cite

View full text Add to dashboard Cite

show abstract

Identifying ubiquitinated proteins and aggregates

Cited by 5 publications

References 5 publications

Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity

Accumulation of “Old Proteins” and the Critical Need for MS‐based Protein Turnover Measurements in Aging and Longevity

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