Co-regulation map of the human proteome enables identification of protein functions
Kustatscher, G; Grabowski, P; Schrader, TA; et al.Passmore, JB; Schrader, M; Rappsilber, J
Date: 4 November 2019
Journal
Nature Biotechnology
Publisher
Nature Research
Publisher DOI
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Abstract
The annotation of protein function is a longstanding challenge of cell biology that
suffers from the sheer magnitude of the task. Here we present ProteomeHD, which
documents the response of 10,323 human proteins to 294 biological perturbations,
measured by isotope-labelling mass spectrometry. We reveal functional associations
between ...
The annotation of protein function is a longstanding challenge of cell biology that
suffers from the sheer magnitude of the task. Here we present ProteomeHD, which
documents the response of 10,323 human proteins to 294 biological perturbations,
measured by isotope-labelling mass spectrometry. We reveal functional associations
between human proteins using the treeClust machine learning algorithm, which we
show to improve protein co-regulation analysis due to robust selectivity for close
linear relationships. Our co-regulation map identifies a functional context for many
uncharacterized proteins, including microproteins that are difficult to study with
traditional methods. Co-regulation also captures relationships between proteins
which do not physically interact or co-localize. For example, co-regulation of the
peroxisomal membrane protein PEX11β with mitochondrial respiration factors led us
to discover a novel organelle interface between peroxisomes and mitochondria in
mammalian cells. The co-regulation map can be explored at www.proteomeHD.net .
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