Cytosolic sorting platform complexes shuttle type III secretion system 
effectors to the injectisome in Yersinia enterocolitica

Wimmi, Stephan; Balinovic, Alexander; Brianceau, Corentin Florian; Pintor, Katherine Lapis; Vielhauer, Jan; Turkowyd, Bartosz; Helbig, Carlos; Fleck, Moritz; Langenfeld, Katja; Kahnt, Jörg; Glatter, Timo; Endesfelder, Ulrike; Diepold, Andreas

doi:10.1038/s41564-023-01545-1

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Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica

MPS-Authors

/persons/resource/persons254844

Wimmi, Stephan
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254115

Balinovic, Alexander
Microbial Networks, Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons269064

Brianceau, Corentin Florian
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons264355

Pintor, Katherine Lapis
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons292891

Vielhauer, Jan
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254776

Turkowyd, Bartosz
Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons263463

Helbig, Carlos
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons263481

Fleck, Moritz
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons219370

Langenfeld, Katja
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254414

Kahnt, Jörg
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons261236

Glatter, Timo
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254244

Endesfelder, Ulrike
Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
external;

/persons/resource/persons254219

Diepold, Andreas
Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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https://doi.org/10.1038/s41564-023-01545-1
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Citation

Wimmi, S., Balinovic, A., Brianceau, C. F., Pintor, K. L., Vielhauer, J., Turkowyd, B., et al. (2024). Cytosolic sorting platform complexes shuttle type III secretion system effectors to the injectisome in Yersinia enterocolitica. Nature Microbiology, 9, 185-199. doi:10.1038/s41564-023-01545-1.

Cite as: https://hdl.handle.net/21.11116/0000-000E-1AA0-0

Abstract

Bacteria use type III secretion injectisomes to inject effector proteins into eukaryotic target cells. Recruitment of effectors to the machinery and the resulting export hierarchy involve the sorting platform. These conserved proteins form pod structures at the cytosolic interface of the injectisome but are also mobile in the cytosol. Photoactivated localization microscopy in Yersinia enterocolitica revealed a direct interaction of the sorting platform proteins SctQ and SctL with effectors in the cytosol of live bacteria. These proteins form larger cytosolic protein complexes involving the ATPase SctN and the membrane connector SctK. The mobility and composition of these mobile pod structures are modulated in the presence of effectors and their chaperones, and upon initiation of secretion, which also increases the number of injectisomes from ~5 to ~18 per bacterium. Our quantitative data support an effector shuttling mechanism, in which sorting platform proteins bind to effectors in the cytosol and deliver the cargo to the export gate at the membrane-bound injectisome.