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Datasets from an interaction proteomics screen for substrates of the SCF(?TrCP) ubiquitin ligase.

ABSTRACT: An affinity purification-mass spectrometry (AP-MS) method was employed to identify novel substrates of the SCF(?TrCP) ubiquitin ligase. A FLAG-HA tagged version of the F-box protein ?TrCP2, the substrate recognition subunit of SCF(?TrCP), was used as bait. ?TrCP2 wild type and the two mutants ?TrCP2-R447A and ?TrCP2-?F were expressed and purified from HEK293T cells to be able to discriminate between potential substrates of SCF(?TrCP) and unspecific binders. Affinity-purified samples were analyzed by mass spectrometry-based proteomics, applying ultra-high performance liquid chromatography (UHPLC) coupled to high-resolution tandem mass spectrometry. The raw mass spectrometry data have been deposited to the PRIDE partner repository with the identifiers PXD001088 and PXD001224. The present dataset is associated with a research resource published in T.Y. Low, M. Peng, R. Magliozzi, S. Mohammed, D. Guardavaccaro, A.J.R. Heck, A systems-wide screen identifies substrates of the SCF(?TrCP) ubiquitin ligase. Sci. Signal. 7 (2014) rs8-rs8, 10.1126/scisignal.2005882.

SUBMITTER: Magliozzi R 

PROVIDER: S-EPMC4510444 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature

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Datasets from an interaction proteomics screen for substrates of the SCF(βTrCP) ubiquitin ligase.

Magliozzi Roberto R   Peng Mao M   Mohammed Shabaz S   Guardavaccaro Daniele D   Heck Albert J R AJ   Low Teck Yew TY  

Data in brief 20150610

An affinity purification-mass spectrometry (AP-MS) method was employed to identify novel substrates of the SCF(βTrCP) ubiquitin ligase. A FLAG-HA tagged version of the F-box protein βTrCP2, the substrate recognition subunit of SCF(βTrCP), was used as bait. βTrCP2 wild type and the two mutants βTrCP2-R447A and βTrCP2-ΔF were expressed and purified from HEK293T cells to be able to discriminate between potential substrates of SCF(βTrCP) and unspecific binders. Affinity-purified samples were analyze  ...[more]

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