Table 1. Published GBP-1-binding partners and GBP-1 functions.
| Binding1 | Function | |
|---|---|---|
| Virus-encoded proteins | ||
| HCV-NSB5 protein | GTPase activity required [49] | Anti-viral [49] |
| IAV-NS1 protein | GTPase activity required [50] | Anti-viral [50] |
| KSHV RTA | n.d. | Anti-viral [51] |
| Cell-encoded proteins | ||
| Actin | n.d.[28]2 | Anti-viral [51]2 |
| PIM1 | Globular and helical domain, partly overlapping with TEAD-binding motif [52] | Improved cell survival, resistance to chemotherapy [52] |
| Plastin-2 [53] | n.d. | n.d. |
| PRL-3 | n.d. | May suppress PRL-3-mediated p53 activity [54] |
| Spectrin β-chain | n.d. | Inhibition of T-cell receptor signaling [53] |
| TEAD | α9-helix of the helical domain3 | Inhibition of cell proliferation3 |
Abbreviations: HCV, Hepatitis C virus; IAV, Influenza A virus; KSHV, Kaposi's sarcoma-associated herpesvirus; n.d., exact binding region and/or impact of binding on function has not been investigated; NS1, nonstructural protein 1; NSB5, nonstructural protein B5; PIM1, proviral integration of Moloney virus 1; PRL, phosphatase of regenerating liver-3; RTA, replication and transcription activator; TEAD, TEA domain protein.
1
Specific binding area or dependence of binding on GTPase activity is given.
2
Own unpublished results suggest that binding occurs in the helical domain, and GTPase activity may modulate binding, inhibiting cell migration and spreading.
3
The results of the present work.