PIM1 is an oncogenic serine/threonine kinase that promotes and maintains prostate
tumorigenesis. To more fully understand the mechanism by which PIM1 promotes oncogenesis,
we performed a chemical genetic screen to identify direct PIM1 substrates in prostate cancer
cells. To identify PIM1 substrates and their phosphorylation sites in LNCaP cells, we coupled a
chemical genetic screen with a peptide capture, mass spectrometry (MS)-based approach. We
mutated the PIM1 gatekeeper residue in the ATP binding site to accept a bulky ATP analog. By
using an ATP analog labeled with a thiol group on the gamma-phosphate, we were able specifically
label PIM1 substrates even in the presence of other cellular kinases.
[doi:10.25345/C5VH73]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: PIM1 substrates ; phosphorylation ; analog-sensitive kinase-substrate detection method
Principal Investigators: (in alphabetical order) |
Beatrix Ueberheide, NYU School of Medicine, USA |
Submitting User: | Trixi |
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Owner | Reanalyses | |
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