Role of intrinsic disorder in transient interactions of hub proteins
- PMID: 17154416
- DOI: 10.1002/prot.21281
Role of intrinsic disorder in transient interactions of hub proteins
Abstract
Hubs in the protein-protein interaction network have been classified as "party" hubs, which are highly correlated in their mRNA expression with their partners while "date" hubs show lesser correlation. In this study, we explored the role of intrinsic disorder in date and party hub interactions. The data reveals that intrinsic disorder is significantly enriched in date hub proteins when compared with party hub proteins. Intrinsic disorder has been largely implicated in transient binding interactions. The disorder to order transition, which occurs during binding interactions in disordered regions, renders the interaction highly reversible while maintaining the high specificity. The enrichment of intrinsic disorder in date hubs may facilitate transient interactions, which might be required for date hubs to interact with different partners at different times.
(c) 2006 Wiley-Liss, Inc.
Similar articles
-
Evolutionary constraints on hub and non-hub proteins in human protein interaction network: insight from protein connectivity and intrinsic disorder.Gene. 2009 Apr 1;434(1-2):50-5. doi: 10.1016/j.gene.2008.12.013. Epub 2008 Dec 29. Gene. 2009. PMID: 19185053
-
Intrinsic disorder of the extracellular matrix.Mol Biosyst. 2011 Dec;7(12):3353-65. doi: 10.1039/c1mb05316g. Epub 2011 Oct 19. Mol Biosyst. 2011. PMID: 22009114
-
Correlation of genomic features with dynamic modularity in the yeast interactome: a view from the structural perspective.IEEE Trans Nanobioscience. 2012 Sep;11(3):244-50. doi: 10.1109/TNB.2012.2212720. IEEE Trans Nanobioscience. 2012. PMID: 22987130
-
Flexible nets. The roles of intrinsic disorder in protein interaction networks.FEBS J. 2005 Oct;272(20):5129-48. doi: 10.1111/j.1742-4658.2005.04948.x. FEBS J. 2005. PMID: 16218947 Review.
-
The role of protein disorder in the 14-3-3 interaction network.Mol Biosyst. 2012 Jan;8(1):178-84. doi: 10.1039/c1mb05216k. Epub 2011 Sep 22. Mol Biosyst. 2012. PMID: 21947246 Review.
Cited by
-
Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding.Protein Sci. 2013 Mar;22(3):258-73. doi: 10.1002/pro.2207. Epub 2013 Jan 27. Protein Sci. 2013. PMID: 23233352 Free PMC article.
-
Isolation and Characterization of Human Colon Adenocarcinoma Stem-Like Cells Based on the Endogenous Expression of the Stem Markers.Int J Mol Sci. 2021 Apr 28;22(9):4682. doi: 10.3390/ijms22094682. Int J Mol Sci. 2021. PMID: 33925224 Free PMC article.
-
Enrichment patterns of intrinsic disorder in proteins.Biophys Rev. 2022 Nov 19;14(6):1487-1493. doi: 10.1007/s12551-022-01016-7. eCollection 2022 Dec. Biophys Rev. 2022. PMID: 36659984 Free PMC article. Review.
-
Conditional disorder in chaperone action.Trends Biochem Sci. 2012 Dec;37(12):517-25. doi: 10.1016/j.tibs.2012.08.006. Epub 2012 Sep 24. Trends Biochem Sci. 2012. PMID: 23018052 Free PMC article. Review.
-
De novo design of bioactive protein switches.Nature. 2019 Aug;572(7768):205-210. doi: 10.1038/s41586-019-1432-8. Epub 2019 Jul 24. Nature. 2019. PMID: 31341284 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources