Top left: Crystal structure of the liprin-α2_CC2N/RIM1_C2B complex. Two neighboring CC2N coiled coils (colored green and gray, respectively), with four bound C2B molecules (colored magenta), are shown. Right inset: Molecular details of interface I formed between the N-terminal part of CC2N and C2B. Salt bridges and hydrogen bonds are indicated by dashed lines. Bottom inset: Molecular details of interface II formed between the C-terminal part of CC2N and C2B. The interconnectivity between interfaces I and II in the complex of one C2B molecule and two CC2N coiled coils is displayed. Salt bridges and hydrogen bonds are indicated by dashed lines. Top right: Surface representation of C2B and CC2N, showing the spatial relationship between the PIP2-binding site and bound CC2N. Key negatively charged residues on the CC2N structure are highlighted in red. Bottom right: Confocal imaging analysis of the LLPS mixture containing the ELKS1/liprin-α2_CC12 (WT or R346E) condensate and the RIM1/RBP2_(SH3)3 condensate. Magnified views of representative RIM1 (a) and ELKS1 (b) droplets were displayed below, with line analyses of fluorescence signal intensities along the indicated lines.
How do scaffolding proteins regulate the assembly of #presynaptic #ActiveZones? This study solves the structure of the liprin-α2/RIM1 complex & shows that it is essential for #synaptic transmission and LLPS-dependent coupling of Ca2+ channels & synaptic vesicles @plosbiology.org 🧪 plos.io/3Tj5CX7