Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation.

Abstract

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.

• Authors: Adrian Mehlitz, Sebastian Banhart, Simone Hess, Matthias Selbach, Thomas F Meyer
• Journal: FEMS microbiology letters (FEMS Microbiol Lett) Vol. 289 Issue 2 Pg. 233-40 (Dec 2008) ISSN: 0378-1097 [Print] England
• PMID: 19016873 (Publication Type: Journal Article)

Chemical References

• Bacterial Proteins
• Phosphoproteins
• Protein Kinases

Topics

• Amino Acid Sequence
• Animals
• Bacterial Proteins (genetics, metabolism)
• Cell Line, Tumor
• Chlamydia Infections (enzymology, microbiology)
• Chlamydia trachomatis (genetics, metabolism)
• HeLa Cells
• Humans
• Mice
• Molecular Sequence Data
• Phosphoproteins (genetics, metabolism)
• Phosphorylation
• Protein Kinases (genetics, metabolism)
• Sequence Alignment