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Protein diversity in discrete structures at the distal tip of the trypanosome flagellum
V. Varga, F. Moreira-Leite, N. Portman, K. Gull,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
Freely Accessible Science Journals od 1915 do Před 6 měsíci
PubMed Central od 1915 do Před 6 měsíci
Europe PubMed Central od 1915 do Před 6 měsíci
Open Access Digital Library od 1915-01-01
Open Access Digital Library od 1915-01-15
Odkazy
PubMed
28724725
DOI
10.1073/pnas.1703553114
Knihovny.cz E-zdroje
- MeSH
- axonema chemie metabolismus MeSH
- flagella chemie metabolismus MeSH
- kineziny chemie metabolismus MeSH
- protozoální proteiny chemie metabolismus MeSH
- Trypanosoma brucei brucei chemie metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The distal end of the eukaryotic flagellum/cilium is important for axonemal growth and signaling and has distinct biomechanical properties. Specific flagellum tip structures exist, yet their composition, dynamics, and functions are largely unknown. We used biochemical approaches to identify seven constituents of the flagella connector at the tip of an assembling trypanosome flagellum and three constituents of the axonemal capping structure at the tips of both assembling and mature flagella. Both tip structures contain evolutionarily conserved as well as kinetoplastid-specific proteins, and component assembly into the structures occurs very early during flagellum extension. Localization and functional studies reveal that the flagella connector membrane junction is attached to the tips of extending microtubules of the assembling flagellum by a kinesin-15 family member. On the opposite side, a kinetoplastid-specific kinesin facilitates attachment of the junction to the microtubules in the mature flagellum. Functional studies also suggest roles of several other components and the definition of subdomains in the tip structures.
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- $a Varga, Vladimir $u Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom; vladimir.varga@img.cas.cz keith.gull@path.ox.ac.uk. Laboratory of Cell Motility, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic.
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- $a The distal end of the eukaryotic flagellum/cilium is important for axonemal growth and signaling and has distinct biomechanical properties. Specific flagellum tip structures exist, yet their composition, dynamics, and functions are largely unknown. We used biochemical approaches to identify seven constituents of the flagella connector at the tip of an assembling trypanosome flagellum and three constituents of the axonemal capping structure at the tips of both assembling and mature flagella. Both tip structures contain evolutionarily conserved as well as kinetoplastid-specific proteins, and component assembly into the structures occurs very early during flagellum extension. Localization and functional studies reveal that the flagella connector membrane junction is attached to the tips of extending microtubules of the assembling flagellum by a kinesin-15 family member. On the opposite side, a kinetoplastid-specific kinesin facilitates attachment of the junction to the microtubules in the mature flagellum. Functional studies also suggest roles of several other components and the definition of subdomains in the tip structures.
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