期刊
JOURNAL OF PROTEOME RESEARCH
卷 8, 期 6, 页码 2978-2989出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr900087r
关键词
Cancer; Chromatin; Phosphorylation; Methylation; Mass spectrometry
资金
- Universita degli Studi di Trieste (Italy)
- Associazione Italiana per la Ricerca sul Cancro (AIRC), Milan (Italy)
HMGA is a family of nuclear proteins involved in a huge number of functions at the chromatin level. It consists of three members, HMGA1a, HMGA1b, and HMGA2, having high sequence homology and sharing the same structural organization (three highly conserved DNA-binding domains, an acidic C-terminal tail, and a protein-protein interaction domain). They are considered important nodes in the chromatin context, establishing a complex network of interactions with both promoter/enhancer sequences and nuclear factors. They are involved in a plethora of biological processes and their activities are finely tuned by several different post-translational modifications. We have performed an LC/MS screening on several different cell lines to investigate HMGA proteins expression and their post-translational modifications in order to detect distinctive modification patterns for each. Our analyses evidenced relevant macroscopic differences in the phosphorylation and methylation patterns of these proteins. These differences occur both within the HMGA family members and in the different cell types. Focusing on HMGA2, we have mapped its in vivo phosphorylation sites demonstrating that, similarly to the HMGA1 proteins, it is highly phosphorylated on the acidic C-terminal tail and that these modifications affect its DNA binding properties.
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