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INS — RASA3
Text-mined interactions from Literome
Cozier et al., J Biol Chem 2000
:
Thus, the Ins ( 1,3,4,5 ) P ( 4 ) -binding PH domain from GAP1(IP4BP) defines a novel class of group I PH domains that constitutively targets the protein to the plasma membrane and may allow
GAP1(IP4BP) to be
regulated in vivo by
Ins ( 1,3,4,5 ) P ( 4 ) rather than PtdIns ( 3,4,5 ) P ( 3 )
Loomis-Husselbee et al., Biochem J 1998
:
We conclude that the increase in
Ins ( 2,4,5 ) P3-stimulated Ca2+ mobilization by Ins ( 1,3,4, 5 ) P4 may be
mediated by
GAP1(IP4BP) or a closely related protein ( such as GAP1 ( m ) ), and if so, the action of the GAP1 is not solely to regulate GTP loading of a G-protein, but rather it acts with a G-protein to cause its effect