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adaptor proteins and their recruited partner proteins aids our un-derstanding of the related signal pathways and their physiologic and binding studies, a report suggested that CCM3 may pre-ferentially heterodimerize with the C-terminal regulatory domain of GCKIII (GCKIIIct) in a manner that is structurally analogousfunctions in the cell (Flynn, 2001; Hunter, 2000; Pan et al., 2012). Loss-of-functionmutations in the adaptor protein CCM3 could lead to cerebral cavernous malformation (CCM), a common to that of CCM3 homodimerization (Ceccarelli et al., 2011). Here, we present the crystal structures of GCKIIIct-CCM3 com-plexes, which provide the precise structural basis for the uniqueINTRODUCTION Adaptor proteins play important roles in numerous signal trans-duction pathways. They often determine the specificity of signaling and also play indispensable roles in the crosstalk of multiple signaling cascades. They can recruit different partner proteins, organize large signaling complexes, and bridg