Evolution of modular intraflagellar transport from a coatomer-like progenitor

  title={Evolution of modular intraflagellar transport from a coatomer-like progenitor},
  author={Teunis J. P. van Dam and Matthew J Townsend and Martina Furdek Turk and Avner Schlessinger and Andrej Sali and Mark C. Field and Martijn A. Huynen},
  journal={Proceedings of the National Academy of Sciences},
  pages={6943 - 6948}
The intraflagellar transport (IFT) complex is an integral component of the cilium, a quintessential organelle of the eukaryotic cell. The IFT system consists of three subcomplexes [i.e., intraflagellar transport (IFT)-A, IFT-B, and the BBSome], which together transport proteins and other molecules along the cilium. IFT dysfunction results in diseases collectively called ciliopathies. It has been proposed that the IFT complexes originated from vesicle coats similar to coat protein complex (COP… 

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The Intraflagellar Transport Machinery.
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Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium.
  • G. Jékely, D. Arendt
  • Biology
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 2006
It is suggested that the initial step in the autogenous origin of the cilium was the establishment of a membrane patch with transmembrane proteins transported by the ancestral vesicle-coating IFT complex, which shares common ancestry with all protocoatomer derivatives, including all vesicles coats and the nuclear pore complex.
The BBSome controls IFT assembly and turnaround in cilia
The results identify the BBSome as the key player regulating IFT assembly and turnaround in cilia and reaches the ciliary tip to regulate proper IFT recycling.
Architecture and function of IFT complex proteins in ciliogenesis.
Dissecting the Sequential Assembly and Localization of Intraflagellar Transport Particle Complex B in Chlamydomonas
A step-wise assembly process for complex B is revealed, and it is shown that the complex first localizes to the proximal end of the centrioles and then translocates onto the transition fibers via an IFT88-dependent mechanism.
Crystal structure of the intraflagellar transport complex 25/27
The crystal structure of Chlamydomonas reinhardtii IFT25/27, an IFT sub‐complex, is determined at 2.6 Å resolution and provides the first step towards a high‐resolution structural understanding of the IFT complex.
Intraflagellar Transport (IFT) Protein IFT25 Is a Phosphoprotein Component of IFT Complex B and Physically Interacts with IFT27 in Chlamydomonas
The identification of a novel IFT particle protein, IFT25, in Chlamydomonas is reported and it is postulate that the association and disassociation between the subcomplex of I FT25 and IFT27 and complex B might be involved in the regulation of IFT.
Stepwise evolution of the centriole-assembly pathway
It is proposed that the UNIMOD theory explains the conservation of CBB architecture and that taxon- and tissue-specific molecular innovations, gained through emergence, duplication and divergence, play important roles in coordinating CBB biogenesis and function in different cellular contexts.
Direct Interactions of Intraflagellar Transport Complex B Proteins IFT88, IFT52, and IFT46*
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Sculpting the endomembrane system in deep time: high resolution phylogenetics of Rab GTPases
A new phylogenetic strategy is devised and exploited to reconstruct the history of the Rab GTPases, a key family of endomembrane-specificity proteins, showing that many Rab paralogues emerged relatively suddenly during early metazoan evolution, which is in stark contrast to the lack of significant Rab family expansions at the onset of most other major eukaryotic groups.