Since its inception in FY2012, the mass spectrometry facility within CPTR collaborated in 15 different projects and analyzed more than 650 samples. Those projects address a variety of biological questions addressed primarily by one of two applications of protein mass spectrometry. One of the most common uses is to identify the entire proteome of a specific sample, such as an organelle, or to identify enriched protein interactors. We have collaborated of seven projects of this type, among them: characterization of the proteome of organelles purified from vegetative and developing Dictyostelium;identification of protein interactors of Arf-GAP proteins;identification of interactors of the delta133 isoform of p53;relative quantitation of secreted proteomes;and protein targets of a small molecule inhibitor. Mass spectrometry analysis is also a leading method to identify sites of post-translational modification on proteins. We have worked on six projects that involve identification protein modifications, including ubiquitination, hosphorylation, methylation, acetylation, and covalent modification by a two different small molecule inhibitors. Currently, many of these projects are still ongoing. Thus far, they have produced very interesting results for the collaborator and suggested specific hypotheses to be tested in follow-up experiments.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Scientific Cores Intramural Research (ZIC)
Project #
1ZICBC011430-01
Application #
8554128
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
1
Fiscal Year
2012
Total Cost
$128,729
Indirect Cost
Name
National Cancer Institute Division of Basic Sciences
Department
Type
DUNS #
City
State
Country
Zip Code
Chaudhary, Ritu; Gryder, Berkley; Woods, Wendy S et al. (2017) Prosurvival long noncoding RNA PINCR regulates a subset of p53 targets in human colorectal cancer cells by binding to Matrin 3. Elife 6:
Chen, Pei-Wen; Jian, Xiaoying; Heissler, Sarah M et al. (2016) The Arf GTPase-activating Protein, ASAP1, Binds Nonmuscle Myosin 2A to Control Remodeling of the Actomyosin Network. J Biol Chem 291:7517-26
Luo, Ruibai; Chen, Pei-Wen; Wagenbach, Michael et al. (2016) Direct functional interaction of the kinesin-13 family member kinesin-like protein 2A (Kif2A) and Arf GAP with GTP-binding protein-like, ankyrin repeats and PH domains 1 (AGAP1). J Biol Chem 291:25761
James, Tamara D; Cardozo, Timothy; Abell, Lauren E et al. (2016) Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase. Nucleic Acids Res 44:7974-88
Kumar, Jeyan S; Miller Jenkins, Lisa M; Gottesman, Michael M et al. (2016) The Drug Excipient Cyclodextrin Interacts With d-Luciferin and Interferes With Bioluminescence Imaging. Mol Imaging 15:
Luo, Ruibai; Chen, Pei-Wen; Wagenbach, Michael et al. (2016) Direct Functional Interaction of the Kinesin-13 Family Membrane Kinesin-like Protein 2A (Kif2A) and Arf GAP with GTP-binding Protein-like, Ankyrin Repeats and PH Domains1 (AGAP1). J Biol Chem 291:21350-21362
Appella, Ettore; Jenkins, Lisa M Miller; Guengerich, F Peter (2015) Introduction to thematic series: protein interactions, structures, and networks. J Biol Chem 290:26393-4
Horikawa, Izumi; Fujita, Kaori; Jenkins, Lisa M Miller et al. (2014) Autophagic degradation of the inhibitory p53 isoform ?133p53? as a regulatory mechanism for p53-mediated senescence. Nat Commun 5:4706
Wang, Rui-Hong; Lahusen, Tyler J; Chen, Qiang et al. (2014) SIRT1 deacetylates TopBP1 and modulates intra-S-phase checkpoint and DNA replication origin firing. Int J Biol Sci 10:1193-202
Hall, Matthew D; Marshall, Travis S; Kwit, Alexandra D T et al. (2014) Inhibition of glutathione peroxidase mediates the collateral sensitivity of multidrug-resistant cells to tiopronin. J Biol Chem 289:21473-89

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