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Cold shock Y-box protein-1 proteolysis autoregulates its transcriptional activities
dc.creator | Van Roeyen, C. R. C. | en |
dc.creator | Scurt, F. G. | en |
dc.creator | Brandt, S. | en |
dc.creator | Kuhl, V. A. | en |
dc.creator | Martinkus, S. | en |
dc.creator | Djudjaj, S. | en |
dc.creator | Raffetseder, U. | en |
dc.creator | Royer, H. D. | en |
dc.creator | Stefanidis, I. | en |
dc.creator | Dunn, S. E. | en |
dc.creator | Dooley, S. | en |
dc.creator | Weng, H. | en |
dc.creator | Fischer, T. | en |
dc.creator | Lindquist, J. A. | en |
dc.creator | Mertens, P. R. | en |
dc.date.accessioned | 2015-11-23T10:53:11Z | |
dc.date.available | 2015-11-23T10:53:11Z | |
dc.date.issued | 2013 | |
dc.identifier | 10.1186/1478-811X-11-63 | |
dc.identifier.issn | 1478811X | |
dc.identifier.uri | http://hdl.handle.net/11615/34281 | |
dc.description.abstract | Background: The Y-box protein-1 (YB-1) fulfills pleiotropic functions relating to gene transcription, mRNA processing, and translation. It remains elusive how YB-1 shuttling into the nuclear and cytoplasmic compartments is regulated and whether limited proteolysis by the 20S proteasome releases fragments with distinct function(s) and subcellular distribution(s). Results: To address these questions, mapping of domains responsible for subcellular targeting was performed. Three nuclear localization signals (NLS) were identified. NLS-1 (aa 149-156) and NLS-2 (aa 185-194) correspond to residues with unknown function(s), whereas NLS-3 (aa 276-292) matches with a designated multimerization domain. Nuclear export signal(s) were not identified. Endoproteolytic processing by the 20S proteasome before glycine 220 releases a carboxy-terminal fragment (CTF), which localized to the nucleus, indicating that NLS-3 is operative. Genotoxic stress induced proteolytic cleavage and nuclear translocation of the CTF. Co-expression of the CTF and full-length YB-1 resulted in an abrogated transcriptional activation of the MMP-2 promoter, indicating an autoregulatory inhibitory loop, whereas it fulfilled similar trans-repressive effects on the collagen type I promoter. Conclusion: Compartmentalization of YB-1 protein derivatives is controlled by distinct NLS, one of which targets a proteolytic cleavage product to the nucleus. We propose a model for an autoregulatory negative feedback loop that halts unlimited transcriptional activation. © 2013 van Roeyen et al.; licensee BioMed Central Ltd. | en |
dc.source.uri | http://www.scopus.com/inward/record.url?eid=2-s2.0-84883580090&partnerID=40&md5=9d8524b9fb135494c75875e877e45e8c | |
dc.subject | Cold shock protein | en |
dc.subject | DbpB | en |
dc.subject | Nuclear localization signal | en |
dc.subject | Post-translational modification | en |
dc.subject | RNA/DNA binding protein | en |
dc.subject | YBX1 | en |
dc.subject | cold shock Y box protein 1 | en |
dc.subject | collagen type 1 | en |
dc.subject | DNA binding protein | en |
dc.subject | gelatinase A | en |
dc.subject | proteasome | en |
dc.subject | RNA binding protein | en |
dc.subject | unclassified drug | en |
dc.subject | nuclear export signal | en |
dc.subject | Y box binding protein 1 | en |
dc.subject | animal cell | en |
dc.subject | article | en |
dc.subject | autoregulation | en |
dc.subject | carboxy terminal sequence | en |
dc.subject | cell compartmentalization | en |
dc.subject | cell nucleus | en |
dc.subject | cellular distribution | en |
dc.subject | nonhuman | en |
dc.subject | priority journal | en |
dc.subject | protein cleavage | en |
dc.subject | protein degradation | en |
dc.subject | protein domain | en |
dc.subject | rat | en |
dc.subject | transcription initiation | en |
dc.subject | animal | en |
dc.subject | cell culture | en |
dc.subject | cell line | en |
dc.subject | chemistry | en |
dc.subject | genetic transcription | en |
dc.subject | human | en |
dc.subject | mesangium cell | en |
dc.subject | metabolism | en |
dc.subject | protein tertiary structure | en |
dc.subject | tumor cell line | en |
dc.subject | Animals | en |
dc.subject | Cell Line, Tumor | en |
dc.subject | Cells, Cultured | en |
dc.subject | Humans | en |
dc.subject | Mesangial Cells | en |
dc.subject | Nuclear Export Signals | en |
dc.subject | Nuclear Localization Signals | en |
dc.subject | Protein Structure, Tertiary | en |
dc.subject | Proteolysis | en |
dc.subject | Rats | en |
dc.subject | Transcription, Genetic | en |
dc.subject | Y-Box-Binding Protein 1 | en |
dc.title | Cold shock Y-box protein-1 proteolysis autoregulates its transcriptional activities | en |
dc.type | journalArticle | en |
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