ArticlePloS one2016
Multiple-Localization and Hub Proteins.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
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- Splicing Modulators Are Involved in Human Polyglutamine Diversification via Protein Complexes Shuttling between Nucleus and Cytoplasm.International journal of molecular sciences · 2023Article
- Computational Methods to Predict Intrinsically Disordered Regions and Functional Regions in Them.Methods in molecular biology (Clifton, N.J.) · 2023Review
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- Signaling pathway network alterations in human ovarian cancers identified with quantitative mitochondrial proteomics.The EPMA journal · 2019Article
- Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins.Biomolecules · 2019Article
- Translocatome: a novel resource for the analysis of protein translocation between cellular organelles.Nucleic acids research · 2019Article
- Both Intrinsically Disordered Regions and Structural Domains Evolve Rapidly in Immune-Related Mammalian Proteins.International journal of molecular sciences · 2018Article
- Surveying the landscape of optogenetic methods for detection of protein-protein interactions.Wiley interdisciplinary reviews. Systems biology and medicine · 2018Review
- Large-scale aggregation analysis of eukaryotic proteins reveals an involvement of intrinsically disordered regions in protein folding.Scientific reports · 2018Article
- Hub Protein Controversy: Taking a Closer Look at Plant Stress Response Hubs.Frontiers in plant science · 2018Review
- Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions.International journal of molecular sciences · 2017Article
- Suppression of MAGE-A10 alters the metastatic phenotype of tongue squamous cell carcinoma cells.Biochemistry and biophysics reports · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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