GBP1 binds actin

Stable Identifier
R-HSA-9956706
Type
Reaction [binding]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Guanylate-binding protein 1 (GBP1), an interferon-γ-inducible large GTPase of the dynamin superfamily, directly binds β-actin, interacting most strongly with globular (G)-actin and to a lesser extent with filamentous (F)-actin. This interaction depends on both the GTPase activity and oligomerization capacity of GBP1 and is sufficient to significantly impair actin filament assembly by sequestering G-actin monomers, thereby reducing the pool of polymerization-competent actin (Ostler N et al., 2014). GBP1-induced cytoskeletal remodeling is believed to impair intracellular trafficking of DNA viruses, such as Kaposi’s sarcoma-associated herpesvirus (KSHV) in humans (Zou Z et al., 2017) and pseudorabies virus (PRV) in swine (Zhang X et al., 2023), by disrupting actin-dependent delivery of viral capsids to the nucleus. Further, mass spectrometry analysis of GBP1 interactomes from Toxoplasma gondii–infected human THP-1 cells revealed enhanced interactions with host actin relative to uninfected cells (Fisch D et al., 2023).
Literature References
PubMed ID Title Journal Year
28592529 Guanylate-Binding Protein 1 Inhibits Nuclear Delivery of Kaposi's Sarcoma-Associated Herpesvirus Virions by Disrupting Formation of Actin Filament

Zou, Z, Meng, Z, Ma, C, Liang, D, Sun, R, Lan, K

J Virol 2017
24190970 Gamma interferon-induced guanylate binding protein 1 is a novel actin cytoskeleton remodeling factor

Ostler, N, Britzen-Laurent, N, Liebl, A, Naschberger, E, Lochnit, G, Ostler, M, Forster, F, Kunzelmann, P, Ince, S, Supper, V, Praefcke, GJ, Schubert, DW, Stockinger, H, Herrmann, C, Stürzl, M

Mol Cell Biol 2014
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!