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ATP5O — GLE1

Text-mined interactions from Literome

Cole et al., Curr Opin Cell Biol 2006 : Gle1 and the phosphoinositide IP6 activate Dbp5 's ATPase activity in vitro and this could provide critical spatial regulation of Dbp5 activity in vivo
Ling et al., RNA Biol 2010 : Biochemical studies show that Gle1 and inositol hexaphosphate ( IP6 ) activate Dbp5 's ATPase activity at the cytoplasmic face of NPC, therefore providing critical spatial regulation of mRNP remodeling during directional transport
Montpetit et al., Nature 2011 : These findings explain how Gle1 ( InsP6 ), Nup159 and Dbp5 collaborate in mRNA export and provide a general mechanism for DEAD-box ATPase regulation by Gle1/eIF4G-like activators
Hodge et al., Genes Dev 2011 : This requires Dbp5 interaction with Nup159 in NPC cytoplasmic filaments and activation of Dbp5 's ATPase activity by Gle1 bound to inositol hexakisphosphate ( IP ( 6 ) )
Noble et al., Genes Dev 2011 : At cytoplasmic NPC filaments, the ATPase activity of DEAD-box protein Dbp5 is activated by inositol hexakisphosphate ( IP ( 6 ) ) -bound Gle1 to mediate remodeling of mRNA-protein ( mRNP ) complexes
Folkmann et al., Nucleus (Austin, Tex.) 2011 : These include a more detailed explanation of the mechanism of Dbp5 RNP remodeling, the role of Gle1-IP6 in stimulating Dbp5 ATPase activity, and the identification of a novel paradigm for regulation of Dbp5 by Nup159