Protein Post-translational Modifications in Disease States

Abstract

Protein function is primarily determined by genomic cording, but further precisely regulated by co- and post-translational modifications. For instance, phosphorylation may be involved in regulation of enzymatic activity, protein interaction with various molecules, cellular localization and so on. Ubiquitination may have significant roles both in protein degradation through proteasome process, and in signal transduction through protein-protein interaction. Therefore, abnormal post-translational modification may disrupt normal cell functions and result in disease states. Actually, phosphorylation of proteins involved in cell growth signaling is upregulated in most cancer cells. Comprehensive proteome analysis based on mass spectrometric technologies are also applicable to detection and identification of post-translational modifications in disease states. Thus, in this review article, I give a brief overview of the recent knowledge about relationship between post-translational modifications and disease states.