Beyond the SNARE: Munc18-1 chaperones α-synuclein.
Early infantile epileptic encephalopathy (EIEE)-associated mutations in MUNC18-1 cause Munc18-1 misfolding and cellular aggregation. In this issue, Chai et al. (2016. J. Cell Biol http://dx.doi.org/10.1083/jcb.201512016) find that Munc18-1 is a molecular chaperone for α-synuclein and that aggregated Munc18-1 EIEE-causing mutants promote α-synuclein aggregation.
Department of Biology, Brandeis University, Waltham, MA 02453.
Mugdha
M
Deshpande
Department of Biology, Brandeis University, Waltham, MA 02453 arodal@brandeis.edu.
Avital A
AA
Rodal
D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics; D009154:Mutation; D011485:Protein Binding; D050600:SNARE Proteins / Q000235:genetics*; D051844:alpha-Synuclein / Q000235:genetics*
D018832:Molecular Chaperones; D050600:SNARE Proteins; D051844:alpha-Synuclein