Tanja Ligensa

Publications (2)20.53 Total impact

• Source

  Available from: PubMed Central

  Article: Negative Regulation of Ros Receptor Tyrosine Kinase Signaling: An Epithelial Function of the Sh2 Domain Protein Tyrosine Phosphatase Shp-1

  Heike Keilhack, Marit Müller, Sylvia-Annette Böhmer, Carsten Frank, K. Michael Weidner, Walter Birchmeier, Tanja Ligensa, Alexander Berndt, Hartwig Kosmehl, Bernd Günther, Thomas Müller, Carmen Birchmeier, Frank-D Böhmer
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  ABSTRACT: Male “viable motheaten” (mev) mice, with a naturally occurring mutation in the gene of the SH2 domain protein tyrosine phosphatase SHP-1, are sterile. Known defects in sperm maturation in these mice correlate with an impaired differentiation of the epididymis, which has similarities to the phenotype of mice with a targeted inactivation of the Ros receptor tyrosine kinase. Ros and SHP-1 are coexpressed in epididymal epithelium, and elevated phosphorylation of Ros in the epididymis of mev mice suggests that Ros signaling is under control of SHP-1 in vivo. Phosphorylated Ros strongly and directly associates with SHP-1 in yeast two-hybrid, glutathione S-transferase pull-down, and coimmunoprecipitation experiments. Strong binding of SHP-1 to Ros is selective compared to six other receptor tyrosine kinases. The interaction is mediated by the SHP-1 NH2-terminal SH2 domain and Ros phosphotyrosine 2267. Overexpression of SHP-1 results in Ros dephosphorylation and effectively downregulates Ros-dependent proliferation and transformation. We propose that SHP-1 is an important downstream regulator of Ros signaling.
  The Journal of Cell Biology 02/2001; · 10.26 Impact Factor
• Source

  Available from: jcb.rupress.org

  Article: Negative Regulation of Ros Receptor Tyrosine Kinase Signaling

  Heike Keilhack, Marit Müller, Sylvia-Annette Böhmer, Carsten Frank, K. Michael Weidner, Walter Birchmeier, Tanja Ligensa, Alexander Berndt, Hartwig Kosmehl, Bernd Günther, Thomas Müller, Carmen Birchmeier, Frank D. Böhmer
  [show abstract] [hide abstract]
  ABSTRACT: Male “viable motheaten” (mev) mice, with a naturally occurring mutation in the gene of the SH2 domain protein tyrosine phosphatase SHP-1, are sterile. Known defects in sperm maturation in these mice correlate with an impaired differentiation of the epididymis, which has similarities to the phenotype of mice with a targeted inactivation of the Ros receptor tyrosine kinase. Ros and SHP-1 are coexpressed in epididymal epithelium, and elevated phosphorylation of Ros in the epididymis of mev mice suggests that Ros signaling is under control of SHP-1 in vivo. Phosphorylated Ros strongly and directly associates with SHP-1 in yeast two-hybrid, glutathione S-transferase pull-down, and coimmunoprecipitation experiments. Strong binding of SHP-1 to Ros is selective compared to six other receptor tyrosine kinases. The interaction is mediated by the SHP-1 NH2-terminal SH2 domain and Ros phosphotyrosine 2267. Overexpression of SHP-1 results in Ros dephosphorylation and effectively downregulates Ros-dependent proliferation and transformation. We propose that SHP-1 is an important downstream regulator of Ros signaling.
  The Journal of Cell Biology 01/2001; 152(2):325-334. · 10.26 Impact Factor