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.
Specific binding area or dependence of binding on GTPase activity is given.
Own unpublished results suggest that binding occurs in the helical domain, and GTPase activity may modulate binding, inhibiting cell migration and spreading.
The results of the present work.