Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin.

ABSTRACT: Chlamydiae are obligate intracellular pathogens that efficiently induce their endocytosis by susceptible eukaryotic host cells. Recently, a Chlamydia trachomatis type III secreted effector protein, Tarp, was found to be translocated and tyrosine phosphorylated at the site of entry and associated with the recruitment of actin that coincides with endocytosis. C. trachomatis Tarp possesses up to six direct repeats of approximately 50 amino acids each. The majority of the tyrosine residues are found within this repeat region. Here we have ectopically expressed distinct domains of Tarp in HeLa 229 cells and demonstrated that tyrosine phosphorylation occurs primarily within the repeat region, while recruitment of actin is mediated by the C-terminal domain of the protein. A comparison of other se

SUBMITTER: Clifton DR 

PROVIDER: S-EPMC1168552 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature