| Literature DB >> 31933212 |
Natania S Field1,2, Claire E O'Leary3, Joseph M Dybas1,2, Hua Ding4, Paula M Oliver5,6.
Abstract
Ubiquitination is a crucial component of many immune processes. While ubiquitin-mediated degradation is essential to T cell activation via T cell receptor signaling, the specific E3 ligases and substrates involved are not well-understood. Here, we describe a strategy integrating RNA, protein, and posttranslational modification datasets to identify targets of ubiquitin-mediated degradation. When integrated, these assays can provide broad insight into how this posttranslational modification regulates protein function and influences T cell biology.Entities:
Keywords: Diglycine remnant profiling; Lymphocyte; Signaling; T cell; Ubiquitin
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Year: 2020 PMID： 31933212 PMCID： PMC7549384 DOI： 10.1007/978-1-0716-0266-9_19
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745