Identification of gasderminD interacting proteins by mass spectrometry

ABSTRACT: Gasdermin D (GSDMD)-mediated macrophage pyroptosis plays a critical role in inflammation and host defense. Plasma membrane perforation elicited by caspase-cleaved GSDMD N-terminal domain (GSDMD-NT) triggers membrane rupture and subsequent pyroptotic cell death, resulting in release of pro-inflammatory IL-1β and IL-18. Here, using a proteomics approach, we identified fatty acid synthase (FASN) as a GSDMD-binding partner and demonstrated that post-translational palmitoylation of GSDMD at Cys191/Cys192 (human/mouse) led to membrane translocation of GSDMD-NT but not full-length GSDMD. Collectively, we establish GSDMD-NT palmitoylation as a key regulatory mechanism modulating immune activity in infectious and inflammatory diseases.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Arumugam Balasubramanian  

LAB HEAD: Hongbo R Luo

PROVIDER: PXD039133 | Pride | 2025-05-06

REPOSITORIES: Pride