Dataset Information

Proteome analysis of Mel426 melanoma cells with R2PD1 treatment

ABSTRACT: A label-free quantification experiment was performed to study the effect of R2PD1 chimeric protein treatment on the cellular proteome of Mel426 human melanoma cells. Peptides were separated by online reverse phase liquid chromatography and measured in an Exploris 480 Orbitrap mass spectrometer. Mass spectrometry raw data were processed by MaxQuant software package (version 2.1.3.0) using its built-in Andromeda search engine. Mass spectra were searched against a target-decoy database consisting of the forward and reverse sequences of UniProt human reference proteome (release 2022_04; 102,601 entries) and a list of 246 common contaminants. Trypsin/P specificity was chosen. The minimum peptide length was set to be 7 amino acids. False discovery rate (FDR) was set to 1% for both peptide and protein identifications. MaxLFQ algorithm was employed for protein quantification.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Christof Niehrs

PROVIDER: MSV000091500 | MassIVE | Thu Mar 16 08:11:00 GMT 2023

SECONDARY ACCESSION(S): PXD040916

REPOSITORIES: MassIVE

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Publications

ROTACs leverage signaling-incompetent R-spondin for targeted protein degradation.

Sun Rui R Meng Zibo Z Lee Hyeyoon H Offringa Rienk R Niehrs Christof C

Cell chemical biology 20230614 7

Proteolysis-targeting chimeras (PROTACs) are an emerging technology for therapeutic intervention, but options to target cell surface proteins and receptors remain limited. Here we introduce ROTACs, bispecific WNT- and BMP-signaling-disabled R-spondin (RSPO) chimeras, which leverage the specificity of these stem cell growth factors for ZNRF3/RNF43 E3 transmembrane ligases, to target degradation of transmembrane proteins. As a proof-of-concept, we targeted the immune checkpoint protein, programmed ...[more]

PMID: 37321224

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