: Proteins do not work alone. Instead, they act as part of complexes, and complexes perform nearly every biological function in the cell. These complexes are held together via protein interactions. With the advent of complete genome sequences, the field of proteomics has developed, allowing proteins and their interactions to be studied on a large-scale basis. The YRC has focused on the analysis of protein complexes for nearly ten years. In doing so, they have developed technologies that have revolutionized the identification of proteins and protein interactions. Through hundreds of collaborations, they successfully applied these new technologies to an array of diverse biological questions. As proteomics comes of age, they will strive to remain at the forefront with a continued focus on protein interactions, advanced through collaborations with the biological community. Their goals are: to develop technologies to quantify proteins and to uncover the mechanisms by which protein interactions are regulated;to develop new affinity tags as well as high throughput methods that allow the identification of interactions without the use of affinity tags;to develop the potential of aptamers as an alternative set of protein specific reagents;to develop computational methods to predict protein interactions, which will proved large-scale function predictions that will be made publicly available for anyone to test;to improve fluorescence resonance energy transfer (FRET) which will allow the description of structures in their native context within living cells;and to combine FRET data with computational approaches in order to predict protein structure and interactions all the way to the atomic level. The multifaceted approach will develop the technologies needed to push biology forward, impacting not just the community of yeast biologists but also those working on all aspects of basic cell biology and human disease research.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR011823-14
Application #
7686386
Study Section
Special Emphasis Panel (ZRG1-CB-H (40))
Program Officer
Tingle, Marjorie
Project Start
1997-09-30
Project End
2011-08-31
Budget Start
2009-09-01
Budget End
2010-08-31
Support Year
14
Fiscal Year
2009
Total Cost
$2,007,027
Indirect Cost
Name
University of Washington
Department
Biochemistry
Type
Schools of Medicine
DUNS #
605799469
City
Seattle
State
WA
Country
United States
Zip Code
98195
Hollmann, Taylor; Kim, Tae Kwon; Tirloni, Lucas et al. (2018) Identification and characterization of proteins in the Amblyomma americanum tick cement cone. Int J Parasitol 48:211-224
Stieg, David C; Willis, Stephen D; Ganesan, Vidyaramanan et al. (2018) A complex molecular switch directs stress-induced cyclin C nuclear release through SCFGrr1-mediated degradation of Med13. Mol Biol Cell 29:363-375
Seixas, Adriana; Alzugaray, María Fernanda; Tirloni, Lucas et al. (2018) Expression profile of Rhipicephalus microplus vitellogenin receptor during oogenesis. Ticks Tick Borne Dis 9:72-81
Wang, Zheng; Wu, Catherine; Aslanian, Aaron et al. (2018) Defective RNA polymerase III is negatively regulated by the SUMO-Ubiquitin-Cdc48 pathway. Elife 7:
Xavier, Marina Amaral; Tirloni, Lucas; Pinto, Antônio F M et al. (2018) A proteomic insight into vitellogenesis during tick ovary maturation. Sci Rep 8:4698
Luhtala, Natalie; Aslanian, Aaron; Yates 3rd, John R et al. (2017) Secreted Glioblastoma Nanovesicles Contain Intracellular Signaling Proteins and Active Ras Incorporated in a Farnesylation-dependent Manner. J Biol Chem 292:611-628
Thakar, Sonal; Wang, Liqing; Yu, Ting et al. (2017) Evidence for opposing roles of Celsr3 and Vangl2 in glutamatergic synapse formation. Proc Natl Acad Sci U S A 114:E610-E618
Jin, Meiyan; Fuller, Gregory G; Han, Ting et al. (2017) Glycolytic Enzymes Coalesce in G Bodies under Hypoxic Stress. Cell Rep 20:895-908
Ogami, Koichi; Richard, Patricia; Chen, Yaqiong et al. (2017) An Mtr4/ZFC3H1 complex facilitates turnover of unstable nuclear RNAs to prevent their cytoplasmic transport and global translational repression. Genes Dev 31:1257-1271
Ju Lee, Hyun; Bartsch, Deniz; Xiao, Cally et al. (2017) A post-transcriptional program coordinated by CSDE1 prevents intrinsic neural differentiation of human embryonic stem cells. Nat Commun 8:1456

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