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Flagellar incorporation of proteins follows at least two different routes in trypanosomes
Author(s) -
Vincensini Laetitia,
Blisnick Thierry,
Bertiaux Eloïse,
Hutchinson Sebastian,
Georgikou Christina,
Ooi CherPheng,
Bastin Philippe
Publication year - 2018
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/boc.201700052
Subject(s) - flagellum , intraflagellar transport , biology , trypanosoma brucei , fluorescence recovery after photobleaching , cilium , dynein , organelle , microbiology and biotechnology , transport protein , biophysics , microtubule , biochemistry , membrane , gene
Background Information Eukaryotic cilia and flagella are sophisticated organelles composed of several hundreds of proteins that need to be incorporated at the right time and the right place during assembly. Results Two methods were used to investigate this process in the model protist Trypanosoma brucei : inducible expression of epitope‐tagged labelled proteins and fluorescence recovery after photobleaching of fluorescent fusion proteins. This revealed that skeletal components of the radial spokes (RSP3), the central pair (PF16) and the outer dynein arms (DNAI1) are incorporated at the distal end of the growing flagellum. They display low or even no visible turnover in mature flagella, a finding further confirmed by monitoring a heavy chain of the outer dynein arm. In contrast, the membrane‐associated protein arginine kinase 3 (AK3) showed rapid turnover in both growing and mature flagella, without particular polarity and independently of intraflagellar transport. Conclusion These results demonstrate different modes of incorporation for structural and membrane‐associated proteins in flagella. Significance The existence of two distinct modes for incorporation of proteins in growing flagella suggests the existence of different targeting machineries. Moreover, the absence of turnover of structural elements supports the view that the length of the mature flagellum in trypanosomes is not modified after assembly.