Identification of TOEFAZ1-interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis.
Mol Microbiol
; 109(3): 306-326, 2018 08.
Article
em En
| MEDLINE
| ID: mdl-29781112
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Trypanosoma brucei brucei
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Glicoproteínas de Membrana
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Proteínas de Protozoários
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Proteínas Serina-Treonina Quinases
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Citocinese
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article