Document Detail

The amino-terminal non-catalytic region of Salmonella typhimurium SigD affects actin organization in yeast and mammalian cells.
MedLine Citation:
PMID:  16153243     Owner:  NLM     Status:  MEDLINE    
The internalization of Salmonella into epithelial cells relies on the function of bacterial proteins which are injected into the cell by a specialized type III secretion system. Such bacterial effectors interfere with host cell signalling and induce local cytoskeletal rearrangements. One of such effectors is SigD/SopB, which shares homology with mammalian inositol phosphatases. We made use of the Saccharomyces cerevisiae model for elucidating new aspects of SigD function. Endogenous expression of SigD in yeast caused severe growth inhibition. Surprisingly, sigD alleles mutated in the catalytic site or even deleted for the whole C-terminal phosphatase domain still inhibited yeast growth by inducing loss of actin polarization and precluding the budding process. Accordingly, when expressed in HeLa cells, the same sigD alleles lost the ability of depleting phosphatidylinositol 4,5-bisphosphate from the plasma membrane, but still caused disappearance of actin fibres and loss of adherence. We delineate a region of 25 amino acids (residues 118-142) that is necessary for the effect of SigD on actin in HeLa cells. Our data indicate that SigD exerts a toxic effect linked to its N-terminal region and independent of its phosphatase activity.
Ainel Alemán; Isabel Rodríguez-Escudero; Gustavo V Mallo; Víctor J Cid; María Molina; Rafael Rotger
Related Documents :
21886563 - Methylone and monoamine transporters: correlation with toxicity.
16773183 - Human dead-box/rna unwindase rck/p54 contributes to maintenance of cell growth by affec...
6302363 - Renal disease profoundly alters cortical interstitial cell function.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cellular microbiology     Volume:  7     ISSN:  1462-5814     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2005 Oct 
Date Detail:
Created Date:  2005-09-12     Completed Date:  2005-12-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1432-46     Citation Subset:  IM    
Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, Spain.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Actins / chemistry,  metabolism*
Bacterial Proteins / genetics,  physiology*
Catalytic Domain
Cell Adhesion
Cells / microbiology*
Fluorescent Antibody Technique
Hela Cells
Microscopy, Fluorescence
Phosphoric Monoester Hydrolases / metabolism
Protein Structure, Tertiary
Saccharomyces cerevisiae / cytology,  genetics,  growth & development
Salmonella typhimurium / physiology*
Sequence Deletion
Reg. No./Substance:
0/Actins; 0/Bacterial Proteins; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.4.-/SopB protein, Salmonella

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Internalization of bacterial redox protein azurin in mammalian cells: entry domain and specificity.
Next Document:  Caspase-1 dependent macrophage death induced by Burkholderia pseudomallei.