English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

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

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.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : J. Cell Sci.

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Gustavsson, A., Author
Armulik, A., Author
Brakebusch, C.1, Author              
Fässler, R.2, Author              
Johansson, S., Author
Fällman, M., Author
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
2Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

Content

show
hide
Free keywords: invasin; beta 1-integrin; Yersinia pseudotuberculosis; focal complexes; bacterial internalization
 Abstract: 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.

Details

show
hide
Language(s): eng - English
 Dates: 2002-07-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41756
ISI: 000176961600006
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Cell Science
  Alternative Title : J. Cell Sci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 115 (13) Sequence Number: - Start / End Page: 2669 - 2678 Identifier: ISSN: 0021-9533