Proteomic identification of proteins conjugated to ISG15 in mouse and human cells
| Autor: | Ernest C. Borden, Barbara S. Jacobs, Herbert W. Virgin, Nadia V. Giannakopoulos, Deborah J. Lenschow, Weiguo Zou, Jun Li, Dong-Er Zhang, Jiann Kae Luo, Vladimir Papov |
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| Rok vydání: | 2005 |
| Předmět: |
Proteomics
Proteome Biophysics Plasma protein binding Biology Biochemistry Peptide Mapping Mass Spectrometry Mice Species Specificity Protein Interaction Mapping Animals Humans Molecular Biology Ubiquitins Cells Cultured Gene Expression Profiling Translation (biology) Cell Biology Transfection Interferon-beta U937 Cells Fibroblasts ISG15 Cell biology Gene expression profiling Mice Inbred C57BL Cytokines Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 336(2) |
| ISSN: | 0006-291X |
| Popis: | Though the interferon-inducible protein ISG15 was one of the first ubiquitin-like modifiers to be discovered, much remains unknown about the identity of proteins conjugated to ISG15 or the biologic consequences of modification. To gain a better understanding of the cellular pathways affected by ISG15, we identified proteins targeted for ISGylation using a proteomic approach. Mass spectrometric analysis identified 76 candidate ISGylation targets in anti-ISG15 immunoprecipitates from interferon-treated mouse or human cells. Twenty-one proteins were found in both mouse and human samples, including STAT1, a known target of ISGylation. Candidates identified in both species were tested for ISGylation in a transfection system: 18 of 19 proteins tested were ISGylated in this system. Two candidates, EF-2 and VCP, were also shown to be ISGylated in an interferon-dependent manner in the absence of exogenous over-expression. Seven proteins identified from a single species, but functionally related to candidates found in both species, were also ISGylated in the over-expression system. Proteins that can be ISGylated play important roles in translation, glycolysis, stress responses, and cell motility. These data indicate that ISGylation targets proteins found in several fundamentally important cellular pathways and will contribute to understanding the physiologic role of interferon-induced ISG15 and ISG15 conjugation. |
| Databáze: | OpenAIRE |
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