The recent completion of the first draft of the human genome marked the beginning of post-genomic science. Genome projects have already catalyzed a new research effort that consists of systematic enumeration and quantification of all the genes and their products expressed in cells or tissue. Quantitative proteomics is an essential tool for protein analysis on a genome-wide scale and will be indispensable for identifying the functions and controls of genes. In particular, protein phosphorylation is the most important posttranslational modification and it plays a critical role in regulating protein functions and numerous biological processes. Large-scale quantitative analysis of protein phosphorylation, in particular, will be very useful in illuminating the phosphorylation networks in complex biological systems. To date, technologies for proteomics-wide analysis of protein phosphorylation have not been established. The work proposed in this application is aimed at the development of proteome technology for a rapid, sensitive, quantitative and comprehensive analysis of protein phosphorylation in complex biological samples. Once developed, such technology will be one of the technological foundations for proteomics and will be a widely applicable tool for biologists' attempts to dissect the functions of genes in their respective research areas.

Agency
National Institute of Health (NIH)
Institute
National Human Genome Research Institute (NHGRI)
Type
Career Transition Award (K22)
Project #
5K22HG002604-03
Application #
6789381
Study Section
Ethical, Legal, Social Implications Review Committee (GNOM)
Program Officer
Felsenfeld, Adam
Project Start
2002-09-30
Project End
2006-08-31
Budget Start
2004-09-01
Budget End
2005-08-31
Support Year
3
Fiscal Year
2004
Total Cost
$269,360
Indirect Cost
Name
Ludwig Institute for Cancer Research
Department
Type
DUNS #
627922248
City
La Jolla
State
CA
Country
United States
Zip Code
92093
Chen, Sheng-hong; Smolka, Marcus B; Zhou, Huilin (2007) Mechanism of Dun1 activation by Rad53 phosphorylation in Saccharomyces cerevisiae. J Biol Chem 282:986-95
Wen, Gen; Wessel, Jennifer; Zhou, Weidong et al. (2007) An ancestral variant of Secretogranin II confers regulation by PHOX2 transcription factors and association with hypertension. Hum Mol Genet 16:1752-64
Enserink, Jorrit M; Smolka, Marcus B; Zhou, Huilin et al. (2006) Checkpoint proteins control morphogenetic events during DNA replication stress in Saccharomyces cerevisiae. J Cell Biol 175:729-41
Smolka, Marcus B; Chen, Sheng-hong; Maddox, Paul S et al. (2006) An FHA domain-mediated protein interaction network of Rad53 reveals its role in polarized cell growth. J Cell Biol 175:743-53
Smolka, Marcus B; Albuquerque, Claudio P; Chen, Sheng-hong et al. (2005) Dynamic changes in protein-protein interaction and protein phosphorylation probed with amine-reactive isotope tag. Mol Cell Proteomics 4:1358-69
Su, Yi-Hsien; Chen, Sheng-Hong; Zhou, Huilin et al. (2005) Tandem mass spectrometry identifies proteins phosphorylated by cyclic AMP-dependent protein kinase when sea urchin sperm undergo the acrosome reaction. Dev Biol 285:116-25
Zhou, Weidong; Ryan, Jennifer J; Zhou, Huilin (2004) Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J Biol Chem 279:32262-8