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Getting tubulin to the tip of the cilium: One IFT train, many different tubulin cargo-binding sites?

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Bhogaraju,  Sagar
Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society;

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Weber,  Kristina
Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Engel,  Benjamin D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Lorentzen,  Esben
Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Bhogaraju, S., Weber, K., Engel, B. D., Lechtreck, K.-F., & Lorentzen, E. (2014). Getting tubulin to the tip of the cilium: One IFT train, many different tubulin cargo-binding sites? BIOESSAYS, 36(5), 463-467. doi:10.1002/bies.201400007.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-8B52-9
Abstract
Cilia are microtubule-based hair-like structures that project from the surfaces of eukaryotic cells. Cilium formation relies on intraflagellar transport (IFT) to move ciliary proteins such as tubulin from the site of synthesis in the cell body to the site of function in the cilium. A large protein complex (the IFT complex) is believed to mediate interactions between cargoes and the molecular motors that walk along axonemal microtubules between the ciliary base and tip. A recent study using purified IFT complexes has identified a tubulin-binding module in the two core IFT proteins IFT74 and IFT81 that likely serves to bind and transport tubulin within cilia. Here, we calculate the amount of tubulin required to support the observed cilium assembly kinetics and explore the possibility of multiple tubulin binding sites within the IFT complex.