Open AccessComplex kinase requirements for Chlamydia trachomatis Tarp phosphorylation
Author(s) -
Mehlitz Adrian,
Banhart Sebastian,
Hess Simone,
Selbach Matthias,
Meyer Thomas F.
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01390.x
Subject(s) - phosphorylation , kinase , syk , microbiology and biotechnology , tyrosine kinase , biology , tyrosine phosphorylation , proto oncogene tyrosine protein kinase src , src family kinase , protein serine threonine kinases , signal transduction , protein kinase a
Chlamydia trachomatis translocates the effector protein Tarp (translocated actin‐recruiting phosphoprotein) into the host cell cytoplasm where it is quickly tyrosine phosphorylated. Abl and Src kinases have been implicated in Tarp phosphorylation; however, we observed that the situation is more complex. Chemical inhibition of Src family kinases confirmed a role for these kinases in Tarp phosphorylation. Infection of Src, Yes, Fyn (SYF)‐deficient cells showed a dampened, but incompletely blocked, Tarp phosphorylation. Inhibition of Abl in an SYF background still did not completely block Tarp phosphorylation. Consequently, we tested additional kinases and found that Syk, but not Btk or Jak2, is a potent kinase of Tarp in vitro . Inhibition of Syk in an SYF background further blocked Tarp phosphorylation. Under these conditions, inclusion formation still proceeded normally. These data reveal a highly promiscuous substrate property of Tarp and set the stage for further functional characterization of Tarp phosphorylation during host cell infection.