Prenylation of an interferon‐γ‐induced GTP‐binding protein: the human guanylate binding protein, huGBP1

@article{Nantais1996PrenylationOA,
  title={Prenylation of an interferon‐$\gamma$‐induced GTP‐binding protein: the human guanylate binding protein, huGBP1},
  author={David E. Nantais and Martin Schwemmle and John T. Stickney and Deborah J. Vestal and Janice E. Buss},
  journal={Journal of Leukocyte Biology},
  year={1996},
  volume={60}
}
Interferons (IFN) and lipopolysaccharide (LPS) cause multiple changes in isoprenoid‐modified proteins in murine macrophages, the most dramatic being the expression of a prenyl protein of 65 kDa. The guanylate binding proteins (GBPs) are IFN‐inducible GTP‐binding proteins of ~65 kDa that possess a CaaX motif at their C‐terminus, indicating that they might be substrates for prenyltransferases. The human GBP1 protein, when expressed in transfected COS‐1 cells, incorporates radioactivity from the… 
Role of GTP binding, isoprenylation, and the C-terminal α-helices in the inhibition of cell spreading by the interferon-induced GTPase, mouse guanylate-binding protein-2.
TLDR
Analysis of variants of mGBP-2 containing amino acid substitutions in the guanosine triphosphate (GTP) binding domain suggests that GTP binding, and possibly dimerization, of mTB-2 is necessary to inhibit cell spreading, however, isoprenylation is also required.
Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein.
TLDR
The results demonstrate that it is possible to alter a protein's prenylation state in a living cell so that graded effects of isoprenoid on function can be studied.
Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor.
TLDR
Evidence is presented that hGBP-1 can associate with the Golgi apparatus and two nonhydrolyzing mutants of hGBp-1, corresponding to active mutants of Ras family proteins, failed to constitutively associate withThe Golgi.
Interferon‐inducible guanylate‐binding proteins at the interface of cell‐autonomous immunity and inflammasome activation
TLDR
An overview on the emerging relationship between GBPs and activation of the inflammasome in innate immunity to microbial pathogens is provided.
Murine GBP-5, a new member of the murine guanylate-binding protein family, is coordinately regulated with other GBPs in vivo and in vitro.
TLDR
A new murine member of the interferon (IFN)-inducible guanylate-binding protein (GBP) family was cloned in a search for glucocorticoid-attenuated response genes induced in the lung during endotoxemia, and coordinate expression of the MuGBPs suggests that they share common mechanisms of regulation.
Mechanisms of negative regulation of protein prenylation: investigation of murine guanylate-binding protein 1
TLDR
The results demonstrate that it is possible to alter a protein's prenylation state in a living cell so that graded effects of isoprenoid on function can be studied.
The IFN-induced GTPase, mGBP-2: Role in IFN-γ induced murine fibroblast proliferation
TLDR
The finding that IFN-γ treatment of NIH 3T3 cells resulted in an increase in proliferation similar to that observed for mGBP-2 in the absence of otherIFN-induced proteins suggests that mGBp-2 may indeed be important for these growth changes.
Identification of GAS‐dependent interferon‐sensitive target genes whose transcription is STAT2‐dependent but ISGF3‐independent
TLDR
This report is the first analysis of the contribution of the STAT2 DNA binding domain to IFN responses on a global basis, and shows that STAT2 is required for the IFN‐inducible activation of the full spectrum of GAS target genes.
Different subcellular localizations for the related interferon-induced GTPases, MuGBP-1 and MuGBP-2: implications for different functions?
  • D. Vestal, V. Gorbacheva, G. Sen
  • Biology
    Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research
  • 2000
TLDR
Reports are reported here on studies to localize both a newly identified murine GBP (MuGBP-2) and its closely related family member, Mu GBP-1, which suggests differential function(s).
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