The endoplasmic reticulum-localized enzyme zDHHC6 mediates S-acylation of short transmembrane constructs from multiple type I and II membrane proteins.

ABSTRACT: In this study, we investigated the S-acylation of two host cell proteins important for viral infection: TMPRSS2 (transmembrane serine protease 2), which cleaves severe acute respiratory syndrome coronavirus 2 spike to facilitate viral entry, and bone marrow stromal antigen 2, a general viral restriction factor. We found that both proteins were S-acylated by zDHHC6, an S-acyltransferase enzyme localized at the endoplasmic reticulum, in coexpression experiments. Mutagenic analysis revealed that zDHHC6 modifies a single cysteine in each protein, which are in proximity to the transmembrane domains (TMDs). For TMPRSS2, the modified cysteine is positioned two residues into the TMD, whereas the modified cysteine in bone marrow stromal antigen 2 has a cytosolic location two amino acids upstream of

SUBMITTER: Salaun C 

PROVIDER: S-EPMC10520890 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature