Daisy Sio‐Seng Lio

Highlights • BAK monomers are activated by C12E8 detergent to form activated dimers • The crystal structure of these activated BAK dimers is described • The structure provides direct evidence for BAK conformational changes on activation • The active dimer has an extended hydrophobic surface that disrupts lipid membranes Summary A body of data supports the existence of core (α2–α5) dimers of BAK and BAX in the oligomeric, membrane-perturbing conformation of these essential apoptotic effector...

The Parkinson's disease (PD)‐causative leucine‐rich repeat kinase 2 (LRRK2) belongs to the Roco family of G‐proteins comprising a Ras‐of‐complex (Roc) domain followed by a C‐terminal of Roc (COR) domain in tandem (called Roc‐COR domain). Two prokaryotic Roc‐COR domains have been characterized as “G proteins activated by guanine nucleotide‐dependent dimerization” (GADs), which require dimerization for activation of their GTPase activity and bind guanine nucleotides with relatively low affinities.