Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches

被引:1
作者
Seo, J
Lee, KJ [1 ]
机构
[1] Ewha Womans Univ, Ctr Cell Signaling Res, Seoul 120750, South Korea
[2] Ewha Womans Univ, Div Mol Life Sci, Seoul 120750, South Korea
[3] Ewha Womans Univ, Coll Pharm, Seoul 120750, South Korea
来源
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2004年 / 37卷 / 01期
关键词
biological function; post-translational modifications; proteomics; mass spectrometry; systemic analysis;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recently produced information on post-translational modifications makes it possible to interpret their biological regulation with new insights. Various protein modifications finely tune the cellular functions of each protein. Understanding the relationship between post-translational modifications. and functional changes ("post-translatomics") is another enormous project, not unlike the human genome project. Proteomics, combined with separation technology and mass spectrometry, makes it possible to dissect and characterize the individual parts of post-translational modifications and provide a systemic analysis. Systemic analysis of post-translational modifications in various signaling pathways has been applied to illustrate the kinetics of modifications. Availability will advance new technologies that improve sensitivity and peptide coverage. The progress of "post-translatomics", novel analytical technologies that are rapidly emerging, offer a great potential for determining the details of the modification sites.
引用
收藏
页码:35 / 44
页数:10
相关论文
共 52 条
[1]   Electrospray ionization and matrix assisted laser desorption/ionization mass spectrometry: Powerful analytical tools in recombinant protein chemistry [J].
Andersen, JS ;
Svensson, B ;
Roepstorff, P .
NATURE BIOTECHNOLOGY, 1996, 14 (04) :449-457
[2]   Phosphopeptide analysis by matrix-assisted laser desorption time-of-flight mass spectrometry [J].
Annan, RS ;
Carr, SA .
ANALYTICAL CHEMISTRY, 1996, 68 (19) :3413-3421
[3]   A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease [J].
Baenziger, JU .
CELL, 2003, 113 (04) :421-422
[4]   Characterization of protein glycosylation by mass spectrometry [J].
Burlingame, AL .
CURRENT OPINION IN BIOTECHNOLOGY, 1996, 7 (01) :4-10
[5]   Selective detection and sequencing of phosphopeptides at the femtomole level by mass spectrometry [J].
Carr, SA ;
Huddleston, MJ ;
Annan, RS .
ANALYTICAL BIOCHEMISTRY, 1996, 239 (02) :180-192
[6]   Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction [J].
Chiarugi, P ;
Cirri, P .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (09) :509-514
[7]  
CHWARTZ JH, 2003, SCI STKE, V190, pPE26
[8]   Sweet 'n' sour: the impact of differential glycosylation on T cell responses [J].
Daniels, MA ;
Hogquist, KA ;
Jameson, SC .
NATURE IMMUNOLOGY, 2002, 3 (10) :903-910
[9]   Electrophoresis combined with novel mass spectrometry techniques: Powerful tools for the analysis of proteins and proteomes [J].
Figeys, D ;
Gygi, SP ;
Zhang, Y ;
Watts, J ;
Gu, M ;
Aebersold, R .
ELECTROPHORESIS, 1998, 19 (10) :1811-1818
[10]   Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes [J].
Fratelli, M ;
Demol, H ;
Puype, M ;
Casagrande, S ;
Eberini, I ;
Salmona, M ;
Bonetto, V ;
Mengozzi, M ;
Duffieux, F ;
Miclet, E ;
Bachi, A ;
Vandekerckhove, J ;
Gianazza, E ;
Ghezzi, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (06) :3505-3510