Global functions of extracellular, transmembrane and cytoplasmic domains of organic solute transporter β-subunit
Probing native metal ion association sites through quenching of fluorophores in the nucleotide-binding domains of the ABC transporter MsbA
α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking
Encephalomyocarditis virus 3C protease attenuates type I interferon production through disrupting the TANK–TBK1–IKKε–IRF3 complex
α-synuclein is an abundant presynaptic protein and, when misfolded, is well known to be involved in neurodegenerative disease such as Parkinson's and Lewy body dementia. However, the normal function of α-synuclein in the brain remains unknown. In this issue of the Biochemical Journal, Lou et al. showed that α-synuclein is able to promote SNARE-dependent vesicles docking by concurrently interacting with the v-SNARE and negatively charged lipid on opposite vesicles. For more information, please see article by Xiaochu Lou et al, pages 2039–2049.