C1QBP mitochondrial interactome

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Discovery

ORGANISM(S): Homo Sapiens

SUBMITTER: Ruibing Chen 

PROVIDER: MSV000079369 | MassIVE | Wed Nov 04 21:02:00 GMT 2015

SECONDARY ACCESSION(S): PXD003148

REPOSITORIES: MassIVE