A fungal ubiquitin ligase and arrestin binding partner contribute to pathogenesis and survival during cellular stress.

ABSTRACT: Cellular responses to external stress allow microorganisms to adapt to a vast array of environmental conditions, including infection sites. The molecular mechanisms behind these responses are studied to gain insight into microbial pathogenesis, which could lead to new antimicrobial therapies. Here, we explore a role for arrestin protein-mediated ubiquitination in stress response and pathogenesis in the pathogenic fungus Cryptococcus neoformans. In a previous study, we identified four arrestin-like proteins in C. neoformans and found that one of these is required for efficient membrane synthesis, likely by directing interaction between fatty acid synthases and the Rsp5 E3 ubiquitin ligase. Here, we further explore Cn Rsp5 function and determine that this single Ub ligas

SUBMITTER: du Plooy LM 

PROVIDER: S-EPMC11481503 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature