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Stat1 nuclear translocation by nucleolin upon monocyte differentiation.

Title: Stat1 nuclear translocation by nucleolin upon monocyte differentiation.
Authors: Uwe Jerke; Sergey Tkachuk; Julia Kiyan; Victoria Stepanova; Angelika Kusch; Michael Hinz; Rainer Dietz; Hermann Haller; Bianca Fuhrman; Inna Dumler
Source: PLoS ONE, Vol 4, Iss 12, p e8302 (2009)
Publisher Information: Public Library of Science (PLoS), 2009.
Publication Year: 2009
Collection: LCC:Medicine; LCC:Science
Subject Terms: Medicine; Science
Description: BackgroundMembers of the signal transducer and activator of transcription (Stat) family of transcription factors traverse the nuclear membrane through a specialized structure, called the nuclear pore complex (NPC), which represents a selective filter for the import of proteins. Karyophilic molecules can bind directly to a subset of proteins of the NPC, collectively called nucleoporins. Alternatively, the transport is mediated via a carrier molecule belonging to the importin/karyopherin superfamily, which transmits the import into the nucleus through the NPC.Methodology/principal findingsIn this study, we provide evidence for an alternative Stat1 nuclear import mechanism, which is mediated by the shuttle protein nucleolin. We observed Stat1-nucleolin association, nuclear translocation and specific binding to the regulatory DNA element GAS. Using expression of nucleolin transgenes, we found that the nuclear localization signal (NLS) of nucleolin is responsible for Stat1 nuclear translocation. We show that this mechanism is utilized upon differentiation of myeloid cells and is specific for the differentiation step from monocytes to macrophages.Conclusions/significanceOur data add the nucleolin-Stat1 complex as a novel functional partner for the cell differentiation program, which is uniquely poised to regulate the transcription machinery via Stat1 and nuclear metabolism via nucleolin.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 1932-6203
Relation: https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0008302
Access URL: https://doaj.org/article/faa4eeef3dbd431c8303e80f4f9f83fc
Accession Number: edsdoj.faa4eeef3dbd431c8303e80f4f9f83fc
Database: Directory of Open Access Journals