GBP1

Guanylate-binding protein 1

Action

Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions:
GTP + H2O = GDP + phosphate

Exhibits antiviral activity against influenza virus.

Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.

GBP-1 is both necessary and sufficient for the inhibitory effects of IFN-γ on cell proliferation, migration, and invasion, as shown in endothelial cells and epithelial tumor cells (17, 19, 34,–37 in [1]).

Purified GBP-1 and actin bound to each other, and this interaction was sufficient to impair the formation of actin filaments in vitro [1].

Cosedimentation and band shift analyses demonstrated that GBP-1 binds robustly to globular actin and slightly to filamentous actin. This indicated that GBP-1 may induce actin remodeling via globular actin sequestering and/or filament capping.[1]..

GBP-1 colocalized with actin at the subcellular level and was both necessary and sufficient for the extensive remodeling of the fibrous actin structure observed in IFN-γ-exposed cells. These effects were dependent on the oligomerization and the GTPase activity of GBP-1[1].

An artificial backwards-moving myosin from three pre-existing molecular building blocks:
- a forward-moving class I myosin motor domain,
- a directional inverter formed by a four-helix bundle segment of human guanylate-binding protein-1
- an artificial lever arm formed by two alpha-actinin repeats.
Reverse-direction movement of myosins can be achieved simply by rotating the direction of the lever arm 180 degrees [2].

Pathways

GBP-1 is a major IFN-γ-induced protein in eukaryotic cells (22, 66 in [1]).

Diseases

Chronic Active Epstein-Barr Virus Infection and Aneurysmal Bone Cysts.

References

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Expression

Upregulated - after 1 hour after exercises and after training.