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2016 ; 11
(6
): e0156455
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Multiple-Localization and Hub Proteins
#MMPMID27285823
Ota M
; Gonja H
; Koike R
; Fukuchi S
PLoS One
2016[]; 11
(6
): e0156455
PMID27285823
show ga
Protein-protein interactions are fundamental for all biological phenomena, and
protein-protein interaction networks provide a global view of the interactions.
The hub proteins, with many interaction partners, play vital roles in the
networks. We investigated the subcellular localizations of proteins in the human
network, and found that the ones localized in multiple subcellular compartments,
especially the nucleus/cytoplasm proteins (NCP), the cytoplasm/cell membrane
proteins (CMP), and the nucleus/cytoplasm/cell membrane proteins (NCMP), tend to
be hubs. Examinations of keywords suggested that among NCP, those related to
post-translational modifications and transcription functions are the major
contributors to the large number of interactions. These types of proteins are
characterized by a multi-domain architecture and intrinsic disorder. A survey of
the typical hub proteins with prominent numbers of interaction partners in the
type revealed that most are either transcription factors or co-regulators
involved in signaling pathways. They translocate from the cytoplasm to the
nucleus, triggered by the phosphorylation and/or ubiquitination of intrinsically
disordered regions. Among CMP and NCMP, the contributors to the numerous
interactions are related to either kinase or ubiquitin ligase activity. Many of
them reside on the cytoplasmic side of the cell membrane, and act as the upstream
regulators of signaling pathways. Overall, these hub proteins function to
transfer external signals to the nucleus, through the cell membrane and the
cytoplasm. Our analysis suggests that multiple-localization is a crucial concept
to characterize groups of hub proteins and their biological functions in cellular
information processing.
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