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Identification of TOEFAZ1‐interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis
Author(s) -
Hilton Nicholas A.,
Sladewski Thomas E.,
Perry Jenna A.,
Pataki Zemplen,
SinclairDavis Amy N.,
Muniz Richard S.,
Tran Holly L.,
Wurster Jenna I.,
Seo Jiwon,
Graffenried Christopher L.
Publication year - 2018
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13986
Subject(s) - cytokinesis , biology , trypanosoma brucei , microbiology and biotechnology , cell division , cleavage furrow , cell cycle protein , cell cycle , genetics , cell , gene
Summary The protist parasite Trypanosoma brucei is an obligate extracellular pathogen that retains its highly polarized morphology during cell division and has evolved a novel cytokinetic process independent of non‐muscle myosin II. The polo‐like kinase homolog TbPLK is essential for transmission of cell polarity during division and for cytokinesis. We previously identified a putative TbPLK substrate named Tip of the Extending FAZ 1 (TOEFAZ1) as an essential kinetoplastid‐specific component of the T. brucei cytokinetic machinery. We performed a proximity‐dependent biotinylation identification (BioID) screen using TOEFAZ1 as a means to identify additional proteins that are involved in cytokinesis. Using quantitative proteomic methods, we identified nearly 500 TOEFAZ1‐proximal proteins and characterized 59 in further detail. Among the candidates, we identified an essential putative phosphatase that regulates the expression level and localization of both TOEFAZ1 and TbPLK, a previously uncharacterized protein that is necessary for the assembly of a new cell posterior, and a microtubule plus‐end directed orphan kinesin that is required for completing cleavage furrow ingression. The identification of these proteins provides new insight into T. brucei cytokinesis and establishes TOEFAZ1 as a key component of this essential and uniquely configured process in kinetoplastids.