C-terminal lysine residues localise NLRP10 at lipid droplets and govern NLRP10 oligomer formation

ABSTRACT: NLRP10 is an atypical member of the NLR family because it lacks a leucine-rich repeat domain at its C-terminus. Here, we show that in human epithelial cells and keratinocytes NLRP10 oligomerises in response to m-3M3FBS and SC-10 treatment. NLRP10 co-localises with ASC upon overexpression, but ASC nucleation and recruitment are different to NLRP3. While neither ATP hydrolysis nor the pyrin domain are required, the C-terminal tail region is both necessary and sufficient for oligomerisation. The generation of chimeric proteins shows that the tail region of human and mouse NLRP10 has a conserved function in oligomerisation but determines different protein stabilities. Changes in the subcellular localisation of NLRP10 and oligomerisation are dependent on the presence of evolutionarily conserved

SUBMITTER: Timo-Daniel Voss 

PROVIDER: S-SCDT-10_1038-S44319-026-00839-9 | biostudies-other |

REPOSITORIES: biostudies-other