Movie 1.

Representation of the three-dimensional (3D) structure of CK1α using the UCSF Chimera software (Pettersen et al., 2021). The ATP-binding Site (Lysin49) is highlighted in red; the active site/proton acceptor (Asp139) is highlighted in magenta. Residue glycine 43 (ck1αG43D), glycine 148 (ck1αG148S) and lysine 141 (ck1αL141M) that are replaced in the three different available mutant ck1α alleles are highlighted in blue. Subsequently, the mutated structure is depicted. The substitution lysine to methionine at position 141 removes an H-bond and favors unfavorable interactions with the active site where atoms are too close together (dashed lines in magenta), highlighted in the last sequence of the video. Labels are located on the upper left side.

CK1α protects WAVE from degradation to regulate cell shape and motility in the immune response

Alexander Hirschhäuser, Marianne van Cann, and Sven Bogdan

J Cell Sci 2021. 134:None-None; doi: 10.1242/jcs.258891