Fig. 5: MEA1 is a bi-handed chaperone with two AP1-recognizing domains.
From: Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1
a AlphaFold-predicted structure of the MEA1-NTD:μ1 dimer using MEA1-NTD (a.a. 1–90) and the a.a. 170–423 of μ1 as input. The CIF file of the predicted structure is included in Supplementary Data 3. b Binding interface between μ1 and MEA1-NTD, corresponding to the dashed box shown in (a). c AlphaFold-predicted structure of the MEA1-CTD:β1 dimer using MEA1-CTD (a.a. 121–185) and the core domain of β1 (a.a. 1–584) as input. The CIF file of the predicted structure is included in Supplementary Data 4. d Binding interface between β1 and MEA1-CTD (a.a. 121–185), corresponding to the dashed box shown in (c). e Diagram illustrating the predicted binding model of MEA1 NTD and CTD to μ1 and β1 subunits. f, g Representative Coomassie blue-stained gels from three independent experiments showing MEA1:AP1 subunit interactions in pull-down assays performed using a setup similar to that in this figure (e). GST and GST-tagged FL μ1 (f) or the core domain of β1 (g) were individually co-expressed with His6-SUMO-tagged MEA1 (FL, NTD, or CTD) in E. coli. Proteins were isolated using nickel beads.
