Dataset Information

Substrate Trapping Proteomics Reveals Targets of the βTrCP2/FBXW11 Ubiquitin Ligase

ABSTRACT: We inhibited the proteosome to ‘trap’ ubiquitylated substrates on the SCFFBXW11 E3 complex. Comparative mass spectrometry analysis of immunopurified FBXW11 protein complexes before and after proteosome inhibition revealed known and putatively novel substrates.

INSTRUMENT(S): LTQ Orbitrap Velos, LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Dennis Goldfarb

LAB HEAD: Michael Ben Major

PROVIDER: PXD001062 | Pride | 2014-10-24

REPOSITORIES: Pride

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Substrate trapping proteomics reveals targets of the βTrCP2/FBXW11 ubiquitin ligase.

Kim Tai Young TY Siesser Priscila F PF Rossman Kent L KL Goldfarb Dennis D Mackinnon Kathryn K Yan Feng F Yi XianHua X MacCoss Michael J MJ Moon Randall T RT Der Channing J CJ Major Michael B MB

Molecular and cellular biology 20141020 1

Defining the full complement of substrates for each ubiquitin ligase remains an important challenge. Improvements in mass spectrometry instrumentation and computation and in protein biochemistry methods have resulted in several new methods for ubiquitin ligase substrate identification. Here we used the parallel adapter capture (PAC) proteomics approach to study βTrCP2/FBXW11, a substrate adaptor for the SKP1-CUL1-F-box (SCF) E3 ubiquitin ligase complex. The processivity of the ubiquitylation rea ...[more]

PMID: 25332235

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			Action	DRS
	042207-HOS-DMSO.RAW	Raw
	042207-HOS-DMSO.pep.xml	Pepxml
	042207-HOS-DMSO.prot.xml	Xml
	042307-HOS-MG132.RAW	Raw
	042307-HOS-MG132.pep.xml	Pepxml