Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin

Kubo, Tomohiro; Brown, Jason; Bellvé, Karl D.; Craige, Branch; Craft, Julie M.; Fogarty, Kevin E.; Lechtreck, Karl‐Ferdinand; Witman, George B.

doi:10.1242/jcs.187120

Cited by 88 publications

(108 citation statements)

References 61 publications

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“…In Chlamydomonas, the expression of an IFT74 version lacking the amino-terminal positively charged region required for high-affinity tubulin binding did not abolish ciliogenesis, but slowed down ciliogenesis (Brown et al 2015). The same was shown to be true also for cells carrying mutations in the CH-domain of IFT81, but when IFT81N and IFT74N were mutated in combination the cells were able to assemble only very short flagella (Kubo et al 2016).…”

Section: Ift81/74 and Ift54 Bind Ab-tubulin Dimers And Mtmentioning

confidence: 87%

The Intraflagellar Transport Machinery

Täschner

Lorentzen

2016

Cold Spring Harb Perspect Biol

301

283

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Eukaryotic cilia and flagella are evolutionarily conserved organelles that protrude from the cell surface. The unique location and properties of cilia allow them to function in vital processes such as motility and signaling. Ciliary assembly and maintenance rely on intraflagellar transport (IFT), the bidirectional movement of a multicomponent transport system between the ciliary base and tip. Since its initial discovery more than two decades ago, considerable effort has been invested in dissecting the molecular mechanisms of IFT in a variety of model organisms. Importantly, IFT was shown to be essential for mammalian development, and defects in this process cause a number of human pathologies known as ciliopathies. Here, we review current knowledge of IFTwith a particular emphasis on the IFT machinery and specific mechanisms of ciliary cargo recognition and transport.

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Section: Ift81/74 and Ift54 Bind Ab-tubulin Dimers And Mtmentioning

confidence: 87%

The Intraflagellar Transport Machinery

Täschner

Lorentzen

2016

Cold Spring Harb Perspect Biol

301

283

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“…First, cargo transport increases dramatically in growing cilia (Craft et al, 2015; Wren et al, 2013), whereas the frequency of IFT is independent of the length of cilia (Dentler, 2005). Second, algae carrying either IFT81 or IFT74 mutants lacking their tubulin-binding domains have greatly reduced tubulin transport rates, but the frequency of anterograde IFT is not significantly affected (Kubo et al, 2016). Nonetheless the dynamic nature of the process necessitates careful kinetic analysis and these hypotheses will require additional detailed tests.…”

Section: Discussionmentioning

confidence: 99%

The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base

et al. 2017

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Summary Highly conserved intraflagellar transport (IFT) protein complexes direct both the assembly of primary cilia and the trafficking of signaling molecules. IFT complexes initially accumulate at the base of the cilium, and periodically enter the cilium suggesting a yet identified mechanism that triggers ciliary entry of IFT complexes. Using AP-MS purification of interactors of the centrosomal and ciliopathy protein, CEP19, we identify CEP350, FOP and the RABL2 GTPase as proteins organizing the first known mechanism directing ciliary entry of IFT complexes. We discover that CEP19 is recruited to the ciliary base by the centriolar CEP350/FOP complex, and then specifically captures GTP-bound RABL2B, which is activated via its intrinsic nucleotide exchange. Activated RABL2B then captures and releases its single effector, the intraflagellar transport B holocomplex, from the large pool of pre-docked IFT-B complexes and thus initiates ciliary entry of IFT.

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“…IFT proteins use their cargobinding sites to transport flagellar precursors for assembly and function (Bhogaraju et al, 2013a,b;Eguether et al, 2014;Ishikawa et al, 2014;Hou et al, 2007;Ahmed et al, 2008;Kubo et al, 2016;Lechtreck, 2015;Wren et al, 2013;Lechtreck et al, 2009;Mukhopadhyay et al, 2010). The I1 dynein complex is preassembled in the cytoplasm as a 20S complex including IC140, IC138, IC97 and other subunits, and then delivered to flagella by IFT with assistance of the adaptor IDA3 (Viswanadha et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…For example, IFT46 directly interacts with ODA16 (also known as DAW1), which facilitates the outer arm dynein transport (Hou et al, 2007;Gao et al, 2010;Ahmed et al, 2008). By dimerization, IFT74 and IFT81 cooperatively transport tubulin for cilia assembly (Kubo et al, 2016;Bhogaraju et al, 2013a). IFT56 appears to transport a set of proteins involved in motility .…”

Section: Introductionmentioning

confidence: 99%

IFT57 stabilizes the assembled intraflagellar transport complex and mediates transport of motility-related flagellar cargo

Jiang

Hernandez

et al. 2017

Journal of Cell Science

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Intraflagellar transport (IFT) is essential for the assembly and maintenance of flagella and cilia. Recent biochemical studies have shown that IFT complex B (IFT-B) is comprised of two subcomplexes, IFT-B1 and IFT-B2. The IFT-B2 subunit IFT57 lies at the interface between IFT-B1 and IFT-B2. Here, using a Chlamydomonas reinhardtii mutant for IFT57, we tested whether IFT57 is required for IFT-B complex assembly by bridging IFT-B1 and IFT-B2 together. In the ift57-1 mutant, levels of IFT57 and other IFT-B proteins were greatly reduced at the whole-cell level. However, strikingly, in the protease-free flagellar compartment, while the level of IFT57 was reduced, the levels of other IFT particle proteins were not concomitantly reduced but were present at the wild-type level. The IFT movement of the IFT57-deficient IFT particles was also unchanged. Moreover, IFT57 depletion disrupted the flagellar waveform, leading to cell swimming defects. Analysis of the mutant flagellar protein composition showed that certain axonemal proteins were altered. Taken together, these findings suggest that IFT57 does not play an essential structural role in the IFT particle complex but rather functions to prevent it from degradation. Additionally, IFT57 is involved in transporting specific motility-related proteins.

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Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin

Cited by 88 publications

References 61 publications

The Intraflagellar Transport Machinery

The Intraflagellar Transport Machinery

The CEP19-RABL2 GTPase Complex Binds IFT-B to Initiate Intraflagellar Transport at the Ciliary Base

IFT57 stabilizes the assembled intraflagellar transport complex and mediates transport of motility-related flagellar cargo

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