This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Elongation factor 2 (EF2) is a key component involved in protein synthesis. Upon phosphorylation by the specific Ca2+/calmodulin-dependent protein kinase EF2 kinase (EF2K), EF2 is completely inactivated. The physiological role of phosphorylation of EF2 is unknown but may involve regulation of cell growth in dividing cells and of local protein synthesis in non-dividing cells. Turnover of EF2K appears to be regulated by its phosphorylation state, possibly by targeting of the enzyme to a ubiquitination/proteosome pathway by phosphorylation of the DSGYPS motif (residues 439-444) by unknown kinases. These kinases may act in concert with PKA to regulate the enzyme. The goal of ongoing studies is to identify protein kinases that are able to phosphorylate EF2K, either within the DSGYPS motif or elsewhere. In the current work, AMP kinase was shown to phosphorylate EF2K. After incubation with the kinase in vitro, EF2K was digested and analyzed by mass spectrometry to discover site(s) of phosphorylation, if any. Our data indicates that EF2K is phosphorylated by AMP kinase at one site within the region 394-400. Work to identify the exact site of phosphorylation is ongoing.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000862-33
Application #
7355047
Study Section
Special Emphasis Panel (ZRG1-BNP (01))
Project Start
2006-03-01
Project End
2007-02-28
Budget Start
2006-03-01
Budget End
2007-02-28
Support Year
33
Fiscal Year
2006
Total Cost
$2,466
Indirect Cost
Name
Rockefeller University
Department
Miscellaneous
Type
Other Domestic Higher Education
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
Manning, Lois R; Popowicz, Anthony M; Padovan, Julio C et al. (2017) Gel filtration of dilute human embryonic hemoglobins reveals basis for their increased oxygen binding. Anal Biochem 519:38-41
Boice, Michael; Salloum, Darin; Mourcin, Frederic et al. (2016) Loss of the HVEM Tumor Suppressor in Lymphoma and Restoration by Modified CAR-T Cells. Cell 167:405-418.e13
Chait, Brian T; Cadene, Martine; Olinares, Paul Dominic et al. (2016) Revealing Higher Order Protein Structure Using Mass Spectrometry. J Am Soc Mass Spectrom 27:952-65
Krutchinsky, Andrew N; Padovan, Júlio C; Cohen, Herbert et al. (2015) Maximizing ion transmission from atmospheric pressure into the vacuum of mass spectrometers with a novel electrospray interface. J Am Soc Mass Spectrom 26:649-58
Mast, Fred D; Rachubinski, Richard A; Aitchison, John D (2015) Signaling dynamics and peroxisomes. Curr Opin Cell Biol 35:131-6
Krutchinsky, Andrew N; Padovan, Júlio C; Cohen, Herbert et al. (2015) Optimizing electrospray interfaces using slowly diverging conical duct (ConDuct) electrodes. J Am Soc Mass Spectrom 26:659-67
Oricchio, Elisa; Papapetrou, Eirini P; Lafaille, Fabien et al. (2014) A cell engineering strategy to enhance the safety of stem cell therapies. Cell Rep 8:1677-1685
Zhong, Yu; Morris, Deanna H; Jin, Lin et al. (2014) Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing Beclin 1-Vps34 complex architecture and reducing intracellular phosphatidylinositol-3 phosphate levels. J Biol Chem 289:26021-37
Mathur, Aabhas; Blais, Steven; Goparaju, Chandra M V et al. (2013) Development of a biosensor for detection of pleural mesothelioma cancer biomarker using surface imprinting. PLoS One 8:e57681
Peterson, Shaun E; Li, Yinyin; Wu-Baer, Foon et al. (2013) Activation of DSB processing requires phosphorylation of CtIP by ATR. Mol Cell 49:657-67

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