scholarly journals Intraflagellar transport proteins 172, 80, 57, 54, 38, and 20 form a stable tubulin‐binding IFT ‐B2 complex

2016 ◽  
Vol 35 (7) ◽  
pp. 773-790 ◽  
Author(s):  
Michael Taschner ◽  
Kristina Weber ◽  
André Mourão ◽  
Melanie Vetter ◽  
Mayanka Awasthi ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Transport Proteins ◽  
Tubulin Binding

Hedgehog signalling in the mouse requires intraflagellar transport proteins

Nature ◽  
2003 ◽  
Vol 426 (6962) ◽  
pp. 83-87 ◽  
Author(s):  
Danwei Huangfu ◽  
Aimin Liu ◽  
Andrew S. Rakeman ◽  
Noel S. Murcia ◽  
Lee Niswander ◽  
...  
Keyword(s):  
Intraflagellar Transport ◽  
Transport Proteins ◽  
Hedgehog Signalling

scholarly journals Diffusion rather than intraflagellar transport likely provides most of the tubulin required for axonemal assembly in Chlamydomonas

2020 ◽  
Vol 133 (17) ◽  
pp. jcs249805 ◽  
Author(s):  
Julie Craft Van De Weghe ◽  
J. Aaron Harris ◽  
Tomohiro Kubo ◽  
George B. Witman ◽  
Karl F. Lechtreck
Keyword(s):  
Binding Site ◽  
Critical Concentration ◽  
Intraflagellar Transport ◽  
Microtubule Assembly ◽  
Strong Reduction ◽  
Tubulin Binding ◽  
Respective Contribution ◽  
Β Tubulin

ABSTRACTTubulin enters the cilium by diffusion and motor-based intraflagellar transport (IFT). However, the respective contribution of each route in providing tubulin for axonemal assembly remains unknown. Using Chlamydomonas, we attenuated IFT-based tubulin transport of GFP–β-tubulin by altering the IFT74N–IFT81N tubulin-binding module and the C-terminal E-hook of tubulin. E-hook-deficient GFP–β-tubulin was incorporated into the axonemal microtubules, but its transport frequency by IFT was reduced by ∼90% in control cells and essentially abolished when the tubulin-binding site of IFT81 was incapacitated. Despite the strong reduction in IFT, the proportion of E-hook-deficient GFP–β-tubulin in the axoneme was only moderately reduced. In vivo imaging showed more GFP–β-tubulin particles entering cilia by diffusion than by IFT. Extrapolated to endogenous tubulin, the data indicate that diffusion provides most of the tubulin required for axonemal assembly. We propose that IFT of tubulin is nevertheless needed for ciliogenesis, because it augments the tubulin pool supplied to the ciliary tip by diffusion, thus ensuring that free tubulin there is maintained at the critical concentration for plus-end microtubule assembly during rapid ciliary growth.

scholarly journals Molecular Basis of Tubulin Transport Within the Cilium by IFT74 and IFT81

Science ◽  
2013 ◽  
Vol 341 (6149) ◽  
pp. 1009-1012 ◽  
Author(s):  
Sagar Bhogaraju ◽  
Lukas Cajanek ◽  
Cécile Fort ◽  
Thierry Blisnick ◽  
Kristina Weber ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Intraflagellar Transport ◽  
Human Cells ◽  
Eukaryotic Cells ◽  
Calponin Homology Domain ◽  
Basic Domain ◽  
Calponin Homology ◽  
Tubulin Binding

Intraflagellar transport (IFT) of ciliary precursors such as tubulin from the cytoplasm to the ciliary tip is involved in the construction of the cilium, a hairlike organelle found on most eukaryotic cells. However, the molecular mechanisms of IFT are poorly understood. Here, we found that the two core IFT proteins IFT74 and IFT81 form a tubulin-binding module and mapped the interaction to a calponin homology domain of IFT81 and a highly basic domain in IFT74. Knockdown of IFT81 and rescue experiments with point mutants showed that tubulin binding by IFT81 was required for ciliogenesis in human cells.

scholarly journals Development of the post-natal growth plate requires intraflagellar transport proteins

2007 ◽  
Vol 305 (1) ◽  
pp. 202-216 ◽  
Author(s):  
Buer Song ◽  
Courtney J. Haycraft ◽  
Hwa-seon Seo ◽  
Bradley K. Yoder ◽  
Rosa Serra
Keyword(s):  
Growth Plate ◽  
Intraflagellar Transport ◽  
Transport Proteins

scholarly journals Diffusion rather than IFT provides most of the tubulin required for axonemal assembly

2018 ◽  
Author(s):  
J. Aaron Harris ◽  
Julie C. Van De Weghe ◽  
Tomohiro Kubo ◽  
George B. Witman ◽  
Karl F. Lechtreck
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Intraflagellar Transport ◽  
Strong Reduction ◽  
Tubulin Binding ◽  
High Concentrations ◽  
Β Tubulin

AbstractTubulin enters the cilia by diffusion and motor-based intraflagellar transport (IFT). The respective contributions of each route in providing tubulin for axonemal assembly are unknown. To attenuate IFT-based transport, we expressed modified GFP-tubulins in strains possessing IFT81 and IFT74 with altered tubulin binding sites. E-hook deficient GFP-β-tubulin normally incorporated into the axonemal microtubules; its transport frequency was reduced by ~90% in control cells and essentially abolished when expressed in a strain possessing IFT81 with an incapacitated tubulin-binding site. Despite the strong reduction in IFT, the share of E-hook deficient GFP-β-tubulin in the axoneme was only moderately reduced indicating that most axonemal tubulin (~80%) enters cilia by diffusion. While not providing the bulk of axonemal tubulin, we propose that motor-based IFT is nevertheless critical for ciliogenesis because it ensures high concentrations of tubulin near the ciliary tip promoting axonemal elongation.

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