Protein phosphorylation by kinases is an important regulatory modification that controls many cellular processes. Advances in tools and approaches to study this modification have greatly expanded the catalog of known phosphorylation sites but there remain substantial gaps in our knowledge. We will apply novel kinome- centric analyses to study canonical cell signaling pathways in order to define pathway-specific signaling modules. Our goal is to develop a mass spectrometry-based phenotyping assay that can identify phosphosignatures of cell signaling.

Public Health Relevance

Our cells use protein phosphorylation to control signaling networks in many cellular processes, both in health and disease. We only know the functional relevance of <3% of phosphorylation sites and powerful analytical methods that constantly expand the catalog of known sites are drastically outpacing our ability to study these important protein modifications. Using novel tools, we will thoroughly characterize cell signaling pathways to learn the most functionally important phosphorylation sites, enabling the development of sensitive and specific clinical diagnostics.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM129090-03
Application #
10115079
Study Section
Cellular Signaling and Regulatory Systems Study Section (CSRS)
Program Officer
Barski, Oleg
Project Start
2019-05-01
Project End
2023-02-28
Budget Start
2021-03-01
Budget End
2022-02-28
Support Year
3
Fiscal Year
2021
Total Cost
Indirect Cost
Name
University of Washington
Department
Pharmacology
Type
Schools of Medicine
DUNS #
605799469
City
Seattle
State
WA
Country
United States
Zip Code
98195