MassIVE MSV000079369

Partial Public PXD003148

C1QBP mitochondrial interactome

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Description

The study of protein-protein interactions is an essential process to understand the biological functions of proteins and the underlying mechanisms. Co-immunoprecipitation coupled with mass spectrometry (CoIP-MS) is one of the most extensively used high-throughput techniques to discover novel protein-protein interactions. However, the traditional CoIP process uses whole cell lysate, disrupts cellular organization, and leads to potential false positives by inducing artificial protein-protein interactions. Here we have developed a strategy by combining subcellular fractionation (SCF) with CoIP -MS to study the interacting proteins of the complement component 1, q subcomponent binding protein (C1QBP) in the mitochondria. Using this method, a novel C1QBP interacting protein, dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (DLAT) was identified and validated. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: C1QBP, AP-MS, protein-protein interaction, mitochondria

Contact

Principal Investigators:
(in alphabetical order) 		Ruibing Chen
Submitting User: RChen

Publications

Chen R, Xiao M, Gao H, Chen Y, Li Y, Liu Y, Zhang N.
Identification of a novel mitochondrial interacting protein of C1QBP using subcellular fractionation coupled with CoIP-MS.
Anal Bioanal Chem. 2016 Feb;408(6):1557-64. Epub 2016 Jan 11.

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