protein
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interact with NGFRAP1, and the interaction occurred in cytoplasm (through N-terminus of VTA1 and the C-terminus of NGFRAP1 (Yu 2007) |
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interacting with CHMP5 (with CHMP5 function in multivesicular body sorting, whereas only VTA1 is required for HIV release) (Ward 2005) |
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VPS4A regulator (Xiao 2008) |
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binds to a different region within CHMP5 than within the other ESCRT-III proteins (Shim 2008) |
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interactions with ESCRT-III proteins may be regulated by ESCRT-III conformation (possible role for direct binding between VTA1 and ESCRT-III proteins that is likely to complement its previously described ability to regulate VPS4A and VPS4B activity) (Shim 2008) |
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interacts with other players of the ESCRT machinery as well as with two known cargo proteins, AQP2 and EGFR, whose degradation is affected upon reduction of VTA1 expression |
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tandem MIT domain of VTA1 binds different types of ESCRT-III proteins, promoting assembly of active VPS4 enzymes on the polymeric ESCRT-III substrate |
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CHMP5(139–195) binds the tandem MIT domain of VTA1 |
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N-terminal domain of VTA1 (LIP5NTD) is required for VTA1-mediated stimulation of VPS4A, and the ESCRT-III protein CHMP5 strongly inhibits the stimulation |
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efficient abscission during cytokinesis requires proper function of the ESCRT-III protein IST1, which binds to the microtubule interacting and trafficking (MIT) domains of VPS4A, VTA1, and SPART via its C-terminal MIT-interacting motif (MIM) |
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interaction between the renal water channel aquaporin-2 (AQP2) and the lysosomal trafficking regulator-interacting protein VTA1 targets AQP2 to multivesicular bodies and facilitates lysosomal degradation |
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