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TitlePIM1 controls GBP1 activity to limit self-damage and to guard against pathogen infection.
Journal, issue, pagesScience, Vol. 382, Issue 6666, Page eadg2253, Year 2023
Publish dateOct 6, 2023
AuthorsDaniel Fisch / Moritz M Pfleiderer / Eleni Anastasakou / Gillian M Mackie / Fabian Wendt / Xiangyang Liu / Barbara Clough / Samuel Lara-Reyna / Vesela Encheva / Ambrosius P Snijders / Hironori Bando / Masahiro Yamamoto / Andrew D Beggs / Jason Mercer / Avinash R Shenoy / Bernd Wollscheid / Kendle M Maslowski / Wojtek P Galej / Eva-Maria Frickel /
PubMed AbstractDisruption of cellular activities by pathogen virulence factors can trigger innate immune responses. Interferon-γ (IFN-γ)-inducible antimicrobial factors, such as the guanylate binding proteins ...Disruption of cellular activities by pathogen virulence factors can trigger innate immune responses. Interferon-γ (IFN-γ)-inducible antimicrobial factors, such as the guanylate binding proteins (GBPs), promote cell-intrinsic defense by attacking intracellular pathogens and by inducing programmed cell death. Working in human macrophages, we discovered that GBP1 expression in the absence of IFN-γ killed the cells and induced Golgi fragmentation. IFN-γ exposure improved macrophage survival through the activity of the kinase PIM1. PIM1 phosphorylated GBP1, leading to its sequestration by 14-3-3σ, which thereby prevented GBP1 membrane association. During infection, the virulence protein TgIST interfered with IFN-γ signaling and depleted PIM1, thereby increasing GBP1 activity. Although infected cells can restrain pathogens in a GBP1-dependent manner, this mechanism can protect uninfected bystander cells. Thus, PIM1 can provide a bait for pathogen virulence factors, guarding the integrity of IFN-γ signaling.
External linksScience / PubMed:37797010 / PubMed Central
MethodsEM (single particle)
Resolution5.12 Å
Structure data

18149

8q4l

EMDB-18149, PDB-8q4l:
GBP1 bound by 14-3-3sigma
Method: EM (single particle) / Resolution: 5.12 Å

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Protein complex / Phosphorylation

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