Mapping proteome-wide interactions of
the fumarate handle. (a)
Cysteine chemoproteomic profiling of EST1027 in C33A cervical cancer
cells using isoDTB-ABPP. C33A cells were treated with DMSO vehicle
or EST1027 (20 μM) for 2 h. Resulting lysates were labeled with
an alkyne-functionalized iodoacetamide probe (IA-alkyne) (200 μM)
for 1 h, after which isotopic desthiobiotin tags were appended by
copper-catalyzed azide–alkyne cycloaddition (CuAAC) and taken
through the isoDTB-ABPP procedure. Shown in blue and red are probe-modified
cysteines that showed control/EST1027 ratios >2 with p < 0.05 from n = 3 biologically independent replicates.
Shown in red is RNF126 C32. (b) Gel-based ABPP of EST1027 against
RNF126. Recombinant RNF126 was preincubated with DMSO vehicle or EST1027
for 30 min prior to labeling of RNF126 with IA-rhodamine (250 nM)
for 1 h. Gels were visualized by in-gel fluorescence, and protein
loading was assessed by silver staining. (c) RNF126 knockdown attenuates
EST1027-mediated CDK4 degradation. RNF126 was stably knocked down
in C33A cells using short hairpin oligonucleotides (shRNF126) compared
to nontargeting shControl oligonucleotides. C33A shControl and shRNF126
cells were treated with DMSO vehicle or EST1027 (5 μM) for 24
h. CDK4, RNF126, and loading control vinculin levels were assessed
by Western blotting. (d) Gel-based ABPP of EST1060 against RNF126
performed as described in (b). (e) Gel-based ABPP of covalent chemical
handles against RNF126 performed as described in (b). (f) Structure
of JP-2-196-alkyne probe. (g) JP-2-196-alkyne labeling of pure RNF126
protein. RNF126 was labeled with DMSO vehicle or JP-2-196-alkyne for
30 min. Probe-modified RNF126 was subjected to CuAAC with a rhodamine-functionalized
azide handle and visualized by SDS/PAGE and in-gel fluorescence. (h)
Competition of JP-2-196-alkyne labeling of RNF126 by JP-2-196. RNF126
pure protein was preincubated with JP-2-196 (50 μM) for 30 min
at 37 °C prior to JP-2-196 labeling (50 μM) for 30 min
at room temperature. Probe-modified RNF126 was subjected to CuAAC
with a rhodamine-functionalized azide handle and visualized by SDS/PAGE
and in-gel fluorescence. (i) JP-2-196-alkyne pulldown proteomics showing
significant and moderately selective engagement of RNF126 and five
additional E3 ubiquitin ligases LRSAM1, RNF40, MID2, RNF219, and RNF14.
HEK293T cells were treated with DMSO vehicle or JP-2-196-alkyne (10
μM) for 6 h. Subsequent lysates were subjected to CuAAC with
an azide-functionalized biotin handle, after which probe-modified
proteins were avidin-enriched, eluted, and digested, and analyzed
by TMT-based quantitative proteomics. Data shown are ratios of JP-2-196-alkyne
vs DMSO-control-enriched proteins and p-values from n = 3 biologically independent replicates/group. Gels and
blots from (b–e,g,h) are representative of n = 3 biologically independent replicates/group.