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 |
| Number of Files: | |
| Total Size: | |
| Spectra: | |
| Subscribers: | |
| Owner | Reanalyses | |
|---|---|---|
| Experimental Design | ||
|
Conditions:
|
||
|
Biological Replicates:
|
||
|
Technical Replicates:
|
||
| Identification Results | ||
|
Proteins (Human, Remapped):
|
||
|
Proteins (Reported):
|
||
|
Peptides:
|
||
|
Variant Peptides:
|
||
|
PSMs:
|
||
| Quantification Results | ||
|
Differential Proteins:
|
||
|
Quantified Proteins:
|
||
| Browse Dataset Files | |
|
FTP Download Link (click to copy):
|