Premium
Multisite protein modifications and their determination by mass spectrometry
Author(s) -
Jensen Ole Noerregaard
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a455-b
Subject(s) - proteomics , posttranslational modification , computational biology , glycosylation , phosphorylation , protein phosphorylation , phosphoproteomics , chemistry , biology , bioinformatics , computer science , biochemical engineering , biochemistry , protein kinase a , engineering , gene , enzyme
The regulatory role of a variety of post‐translational modifications of proteins and the significance of the functional interplay between modifications is now only beginning to be realized and worldwide much research is being directed towards this goal. Progress in this field of research relies on availability of sensitive and specific analytical techniques to monitor and establish the nature of modifications on proteins and the dynamic changes they undergo, in health and disease. A completely new set of analytical strategies and technologies have to be developed and applied in biological and biomedical studies. We are using the concept of ‘modification‐specific’ proteomics to investigate protein phosphorylation, glycosylation, acylation and other types of post‐translational modifications. We have recently reported on a quantitative phosphoproteomic study of the yeast pheromone signaling pathway, where more than 700 phosphopeptides were identified, among which 131 could be quantified. This study demonstrated that it is feasible to monitor cell signaling processes as a response to environmental factors, such as hormones. The concept of ‘modification‐specific proteomics’ will be presented as will several applications to biological systems.