Imperial College London
Alternate

ProfessorDavidHolden

Faculty of Medicine, Department of Infectious Disease

Professor
 
 
 
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Contact

 

+44 (0)20 7594 3073d.holden

 
 
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Location

 

221Flowers buildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Domingues:2016:10.1111/cmi.12558,
author = {Domingues, L and Ismail, A and Charro, N and Rodriguez-Escudero, I and Holden, DW and Molina, M and Cid, VJ and Mota, LJ},
doi = {10.1111/cmi.12558},
journal = {Cellular Microbiology},
pages = {949--969},
title = {The Salmonella effector SteA binds phosphatidylinositol 4-phosphate for subcellular targeting within host cells},
url = {http://dx.doi.org/10.1111/cmi.12558},
volume = {18},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Many bacterial pathogens use specialized secretion systems to deliver virulence effector proteins into eukaryotic host cells. The function of these effectors depends on their localization within infected cells, but the mechanisms determining subcellular targeting of each effector are mostly elusive. Here, we show that the Salmonella type III secretion effector SteA binds specifically to phosphatidylinositol 4-phosphate [PI(4)P]. Ectopically expressed SteA localized at the plasma membrane (PM) of eukaryotic cells. However, SteA was displaced from the PM of Saccharomyces cerevisiae in mutants unable to synthesize the local pool of PI(4)P and from the PM of HeLa cells after localized depletion of PI(4)P. Moreover, in infected cells, bacterially translocated or ectopically expressed SteA localized at the membrane of the Salmonella-containing vacuole (SCV) and to Salmonella-induced tubules; using the PI(4)P-binding domain of the Legionella type IV secretion effector SidC as probe, we found PI(4)P at the SCV membrane and associated tubules throughout Salmonella infection of HeLa cells. Both binding of SteA to PI(4)P and the subcellular localization of ectopically expressed or bacterially translocated SteA were dependent on a lysine residue near the N-terminus of the protein. Overall, this indicates that binding of SteA to PI(4)P is necessary for its localization within host cells.
AU  - Domingues,L
AU  - Ismail,A
AU  - Charro,N
AU  - Rodriguez-Escudero,I
AU  - Holden,DW
AU  - Molina,M
AU  - Cid,VJ
AU  - Mota,LJ
DO  - 10.1111/cmi.12558
EP  - 969
PY  - 2016///
SN  - 1462-5822
SP  - 949
TI  - The Salmonella effector SteA binds phosphatidylinositol 4-phosphate for subcellular targeting within host cells
T2  - Cellular Microbiology
UR  - http://dx.doi.org/10.1111/cmi.12558
VL  - 18
ER  -
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