Assembly mechanism of Trypanosoma brucei BILBO1 at the flagellar pocket collar

Commun Integr Biol. 2015 Jan 28;8(1):e992739. doi: 10.4161/19420889.2014.992739. eCollection 2015 Jan-Feb.

Abstract

The flagellar pocket is a bulb-like invagination of the plasma membrane that encloses the base of the single flagellum in trypanosomes. It is the site of all endo- and exocytic activity in the parasite and has thus been proposed to be a therapeutic target. At the neck of the flagellar pocket is an electron-dense cytoskeletal structure named the flagellar pocket collar. The protein BILBO1 was the first characterized and remains the only known component of the flagellar pocket collar, with essential functions in the biogenesis of both the flagellar pocket and flagellar pocket collar. We recently reported that the filamentous assembly of Trypanosoma brucei BILBO1 (TbBILBO1) is mediated by its central coiled coil domain and C-terminal leucine zipper. Here, we discuss how TbBILBO1 might assemble at the flagellar pocket collar in T. brucei.

Keywords: BILBO1; Trypanosoma brucei; cytoskeleton; flagellar pocket; flagellar pocket collar; parasite; protein assembly.