STAT1 from the cell membrane to the DNA

Lillemeier, Björn F.; Köster, Mario; Kerr, Ian M.

doi:10.1093/emboj/20.10.2508

Cited by 88Cytokine Signaling Pathways and Interactionsinterferon and immune responsesNuclear Structure and Function

STAT1 from the cell membrane to the DNA

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Lillemeier, Björn F., Köster, Mario, Kerr, Ian M.·2001·The EMBO Journal

DOI 10.1093/emboj/20.10.2508PMC PMC125461

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Abstract

The binding of interferons (IFNs) to their receptors leads to the phosphorylation and activation of signal transducers and activators of transcription (STATs), and their translocation from the cytoplasm to the nucleus. The mechanisms by which the STATs move to the nuclear pore are not, however, known. Here it is shown that IFN-alpha and -gamma signalling and STAT1 translocation are independent of the actin cytoskeleton or microtubules. Using fluorescence loss in photobleaching (FLIP) and fluorescence recovery after photobleaching (FRAP) experiments, the mobility of a fusion protein of STAT1 with green fluorescent protein (STAT1-GFP) was compared with that of GFP and protein kinase C-GFP. In IFN-gamma-treated and control cells, cytoplasmic STAT1-GFP shows high, energy-independent, mobility comparable to that of freely diffusible GFP. A random walk model for movement of STAT1 from the plasma membrane to the nuclear pore is, therefore, indicated. Nuclear STAT1-GFP showed similar high mobility, with exclusion from nucleoli, consistent with high rates of association and dissociation of STAT1-DNA and/or STAT1-protein complexes in the nucleoplasm of the cell.

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The mobility of Stat1 is much faster than core histones and similar to other inducible transcriptional regulators.
“Compared with other studies, the mobility of Stat1 was much faster than the core histones and similar to other inducible transcriptional regulators (McNally et al. 2000; Kimura and Cook 2001; Lillemeier et al. 2001).”
From DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1 (2003) · cites this paper as Lillemeier et al. 2001
The Discussion (page unavailable) describes STAT1–GFP as highly mobile and compares its dynamic interactions with those of the glucocorticoid receptor, an inducible transcriptional regulator. It does not compare STAT1 mobility with that of core histones, so that part of the claim is not supported by this paper. (LLM, conf=0.84)
Experimental — accuracy not yet measured
The analysis of nucleocytoplasmic transport of Stat1 has revealed its high, energy-independent mobility in the cytoplasm, indicative of random diffusion.
“The analysis of nucleocytoplasmic transport of Stat1 has revealed its high, energy-independent mobility in the cytoplasm, which is indicative of random diffusion (Lillemeier et al. 2001).”
From DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1 (2003) · cites this paper as Lillemeier et al. 2001

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Authors: Lillemeier, B. F., Köster, M., & Kerr, I. M.
Affiliations: Helmholtz Centre for Infection Research (DE)
Corresponding author: Kerr, Ian M.
ORCID: Lillemeier, Björn F.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2001-05-15
Volume: 20
Issue: 10
Pages: 2508-2517
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1093/emboj/20.10.2508
PMC: PMC125461
OpenAlex: W2024998142
Cited by: 88
References: 52
Citations by year: 2024: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2017: 2 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 1 · 2012: 4
FWCI: 5.61
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
Funders: Israel Cancer Research Fund
Topics: Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: STAT1, interferon signaling, interferon-gamma, interferon-alpha, nuclear translocation, nuclear pores, protein diffusion, microtubules, signal transducer and activator of transcription
MeSH terms: Interferon gamma Receptor, Biological Transport, Cell Membrane, Cell Nucleolus, Cell Nucleus, Cytoplasm, Cytoskeleton, DNA, DNA-Binding Proteins, Fluorescence, Humans, Interferon-gamma, Membrane Proteins, Recombinant Fusion Proteins, Tumor Cells, Cultured, Signal Transduction, Trans-Activators, Interferon-alpha, Receptors, Interferon, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase 8, Mitogen-Activated Protein Kinase 9, STAT1 Transcription Factor, Receptor, Interferon alpha-beta

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