{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,3]],"date-time":"2026-11-03T02:53:28Z","timestamp":1793674408357,"version":"4.5.1"},"reference-count":58,"publisher":"The Company of Biologists","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>The Trypanosoma brucei flagellum is an essential organelle anchored along the surface of the cell body via a specialized structure called the flagellum attachment zone (FAZ). Adhesion relies on the interaction of the extracellular portion of two transmembrane proteins termed FLA1 and FLA1BP. Analysis of the flagellum proteome identified FLAM3, a novel large protein associated to the flagellum skeleton whose ablation inhibits flagellum attachment. FLAM3 does not contain transmembrane domains and its flagellar localization matches closely but not exactly with that of the paraflagellar rod, an extra-axonemal structure present in the flagellum. Knockdown of FLA1 or FLAM3 triggers similar motility and morphogenesis defects, characterized by the assembly of a drastically reduced FAZ filament. FLAM3 remains associated to the flagellum skeleton even in the absence of adhesion or of a normal paraflagellar rod. However, the protein is dispersed in the cytoplasm when flagellum formation is inhibited. By contrast, FLA1 remains tightly associated to the FAZ filament even in the absence of a flagellum. In these conditions, the extracellular domain of FLA1 points to the cell surface. FLAM3 turns out to be essential for proper distribution of FLA1BP that is restricted to the very proximal portion of the flagellum upon FLAM3 knockdown. We propose that FLAM3 is a key component of the FAZ connectors that appear to link the axoneme to the adhesion zone, hence acting in an equivalent manner to the FAZ filament complex, but on the flagellum side.<\/jats:p>","DOI":"10.1242\/jcs.136424","type":"journal-article","created":{"date-parts":[[2013,10,25]],"date-time":"2013-10-25T22:42:06Z","timestamp":1382740926000},"source":"Crossref","is-referenced-by-count":38,"title":["Flagellar adhesion in\n                    <i>Trypanosoma brucei<\/i>\n                    relies on interactions between different skeletal structures present in the flagellum and in the cell body"],"prefix":"10.1242","author":[{"given":"Brice","family":"Rotureau","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thierry","family":"Blisnick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ines","family":"Subota","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daria","family":"Julkowska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nad\u00e8ge","family":"Cayet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sylvie","family":"Perrot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe","family":"Bastin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2013,1,1]]},"reference":[{"key":"2021042613214999000_b1","doi-asserted-by":"publisher","first-page":"e437","DOI":"10.1371\/journal.pone.0000437","article-title":"Basal body positioning is controlled by flagellum formation in Trypanosoma brucei.","volume":"2","author":"Absalon","year":"2007","journal-title":"PLoS ONE"},{"key":"2021042613214999000_b2","doi-asserted-by":"publisher","first-page":"929","DOI":"10.1091\/mbc.E07-08-0749","article-title":"Intraflagellar transport and functional analysis of genes required for flagellum formation in trypanosomes.","volume":"19","author":"Absalon","year":"2008","journal-title":"Mol. 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