Abstract:
:Gamma interferon (IFN-γ) regulates immune defenses against viruses, intracellular pathogens, and tumors by modulating cell proliferation, migration, invasion, and vesicle trafficking processes. The large GTPase guanylate binding protein 1 (GBP-1) is among the cellular proteins that is the most abundantly induced by IFN-γ and mediates its cell biologic effects. As yet, the molecular mechanisms of action of GBP-1 remain unknown. Applying an interaction proteomics approach, we identified actin as a strong and specific binding partner of GBP-1. Furthermore, 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. Purified GBP-1 and actin bound to each other, and this interaction was sufficient to impair the formation of actin filaments in vitro, as demonstrated by atomic force microscopy, dynamic light scattering, and fluorescence-monitored polymerization. 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. These results establish GBP-1 as a novel member within the family of actin-remodeling proteins specifically mediating IFN-γ-dependent defense strategies.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
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 Mdoi
10.1128/MCB.00664-13subject
Has Abstractpub_date
2014-01-01 00:00:00pages
196-209issue
2eissn
0270-7306issn
1098-5549pii
MCB.00664-13journal_volume
34pub_type
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