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Role of the beta 1-integrin cytoplasmic tail in mediating invasin-promoted internalization of Yersinia

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77799

Brakebusch,  C.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77945

Fässler,  R.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Gustavsson, A., Armulik, A., Brakebusch, C., Fässler, R., Johansson, S., & Fällman, M. (2002). Role of the beta 1-integrin cytoplasmic tail in mediating invasin-promoted internalization of Yersinia. Journal of Cell Science, 115(13), 2669-2678.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6ED4-3
Zusammenfassung
Invasin of Yersinia pseudotuberculosis binds to beta1-integrins on host cells and triggers internalization of the bacterium. To elucidate the mechanism behind the beta1-integrin-mediated internalization of Yersinia, a beta1-integrin-deficient cell line, GD25, transfected with wild-type beta1A, beta1B or different mutants of the beta1A subunit was used. Both beta1A and beta1B bound to invasin-expressing bacteria, but only beta1A was able to mediate internalization of the bacteria. The cytoplasmic region of beta1A, differing from beta1B, contains two NPXY motifs surrounding a double threonine site. Exchanging the tyrosines of the two NPXYs to phenylalanines did not inhibit the uptake, whereas a marked reduction was seen when the first tyrosine (Y783) was exchanged to alanine. A similar reduction was seen when the two nearby threonines (TT788-9) were exchanged with alanines. It was also noted that cells affected in bacterial internalization exhibited reduced spreading capability when seeded onto invasin, suggesting a correlation between the internalization of invasin-expressing bacteria and invasin-induced spreading. Likewise, integrins defective in forming peripheral focal complex structures was unable to mediate uptake of invasin-expressing bacteria.