Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization

Bizet, Albane A.; Becker-Heck, Anita; Ryan, Rebecca; Weber, Kristina; Filhol, Emilie; Krug, Pauline; Halbritter, Jan; Delous, Marion; Lasbennes, Marie-Christine; Linghu, Bolan; Oakeley, Edward J.; Zarhrate, Mohammed; Nitschké, Patrick; Garfa-Traoré, Meriem; Serluca, Fabrizio C.; Yang, Fan; Bouwmeester, Tewis; Pinson, Lucile; Cassuto, Élisabeth; Dubot, P; Soliman, Neveen A.; Sahel, José‐Alain; Salomon, Rémi; Drummond, Iain A.; Gubler, Marie–Claire; Antignac, Corinne; Chibout, Salah-Dine; Szustakowski, Joseph D.; Hildebrandt, Friedhelm; Lorentzen, Esben; Sailer, Andreas W.; Benmerah, Alexandre; Saint-Mézard, Pierre; Saunier, Sophie

doi:10.1038/ncomms9666

Cited by 87 publications

(95 citation statements)

References 52 publications

(71 reference statements)

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“…Since four of the seven interactors share biological functions with IFT20, we considered them as bona fide IFT20 functional partners. IFT54 and GMAP-210 have been previously described as IFT20 interactors in ciliated cells (Follit et al, 2008(Follit et al, , 2009Bizet et al, 2015). This interaction was found to extend to T cells, as assessed by pulldown assays.…”

Section: Discussionmentioning

confidence: 80%

“…ARPC3 is a component of Arp2/3 complex that is involved in F-actin nucleation and it is known to participate in IS assembly . IFT54 is part of the IFT-B complex, which includes IFT20, IFT57 and IFT88 and is required for ciliogenesis, but it has also been implicated in microtubule stability (Bizet et al, 2015;Berbari et al, 2011;Guo et al, 2010;Follit et al, 2009). The golgin GMAP-210 is a known IFT20 interactor in ciliated cells, where it has been shown to tether IFT20 to the Golgi (Follit et al, 2006;Follit et al, 2008).…”

Section: Identification Of Novel Ift20 Interactors By Mass Spectrometrymentioning

confidence: 99%

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The T cell IFT20 interactome reveals new players in immune synapse assembly

Galgano

Onnis

Pappalardo

et al. 2017

Journal of Cell Science

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Sustained signalling at the immune synapse (IS) requires the synaptic delivery of recycling endosome-associated T cell antigen receptors (TCRs). IFT20, a component of the intraflagellar transport system, controls TCR recycling to the IS as a complex with IFT57 and IFT88. Here, we used quantitative mass spectrometry to identify additional interaction partners of IFT20 in Jurkat T cells. In addition to IFT57 and IFT88, the analysis revealed new binding partners, including IFT54 (also known as TRAF3IP1), GMAP-210 (also known as TRIP11), Arp2/3 complex subunit-3 (ARPC3), COP9 signalosome subunit-1 (CSN1, also known as GPS1) and ERGIC-53 (also known as LMAN1). A direct interaction between IFT20 and both IFT54 and GMAP-210 was confirmed in pulldown assays. Confocal imaging of antigen-specific conjugates using T cells depleted of these proteins by RNA interference showed that TCR accumulation and phosphotyrosine signalling at the IS were impaired in the absence of IFT54, ARPC3 or ERGIC-53. Similar to in IFT20-deficient T cells, this defect resulted from a reduced ability of endosomal TCRs to polarize to the IS despite a correct translocation of the centrosome towards the antigen-presenting cell contact. Our data underscore the traffic-related role of an IFT20 complex that includes components of the intracellular trafficking machinery in IS assembly.

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Section: Discussionmentioning

confidence: 80%

Section: Identification Of Novel Ift20 Interactors By Mass Spectrometrymentioning

confidence: 99%

The T cell IFT20 interactome reveals new players in immune synapse assembly

Galgano

Onnis

Pappalardo

et al. 2017

Journal of Cell Science

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“…In support of this notion, mouse IFT54 mutant cell lines showed an accumulation of acetylated MTs in the cytoplasm (Berbari et al , 2011). Additionally, IFT54 mutations in ciliopathy patients facilitated the characterization of an IFT54 function in the regulation of cytoplasmic MT dynamics (Bizet et al , 2015). Interestingly, several IFT proteins cluster at the spindle of dividing cells and are required for proper formation of astral MTs (Delaval et al , 2011).…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2016

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Intraflagellar transport (IFT) relies on the IFT complex and is required for ciliogenesis. The IFT‐B complex consists of 9–10 stably associated core subunits and six “peripheral” subunits that were shown to dissociate from the core structure at moderate salt concentration. We purified the six “peripheral” IFT‐B subunits of Chlamydomonas reinhardtii as recombinant proteins and show that they form a stable complex independently of the IFT‐B core. We suggest a nomenclature of IFT‐B1 (core) and IFT‐B2 (peripheral) for the two IFT‐B subcomplexes. We demonstrate that IFT88, together with the N‐terminal domain of IFT52, is necessary to bridge the interaction between IFT‐B1 and B2. The crystal structure of IFT52N reveals highly conserved residues critical for IFT‐B1/IFT‐B2 complex formation. Furthermore, we show that of the three IFT‐B2 subunits containing a calponin homology (CH) domain (IFT38, 54, and 57), only IFT54 binds αβ‐tubulin as a potential IFT cargo, whereas the CH domains of IFT38 and IFT57 mediate the interaction with IFT80 and IFT172, respectively. Crystal structures of IFT54 CH domains reveal that tubulin binding is mediated by basic surface‐exposed residues.

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“…The regulated expression of bivalve TRAF3s in response to bacterial challenge that has been revealed in these studies implies the involvement of TRAF3 and its related molecules in innate immunity of shellfish. However, as a protein that interacts specifically with TRAF3, TRAF3IP1 has mainly been identified in mammals (Ling and Goeddel, 2000;Bizet et al, 2015) and also in model organisms such as Caenorhabditis elegans (Kunitomo and Iino, 2007), but its characterization, expression pattern or possible function in marine invertebrates has not been reported.…”

Section: Introductionmentioning

confidence: 99%

Characterization of the <i>TRAF3IP1</i> gene in Yesso scallop (<i>Patinopecten yessoensis</i>) and its expression in response to bacterial challenge

Cheng

Wang

et al. 2016

Genes Genet. Syst.

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Tumor necrosis factor receptor-associated factor 3 (TRAF3) is an important adaptor that transmits upstream activation signals to induce innate immune responses. TRAF3 interacting protein 1 (TRAF3IP1) interacts specifically with TRAF3, but its function in innate immunity remains unclear, especially in marine invertebrates. In this study, to better understand the functions of TRAFs in innate immune responses, we identified and characterized the first bivalve TRAF3IP1 gene, PyTRAF3IP1, from Yesso scallop (Patinopecten yessoensis), one of the most important mollusk species for aquaculture. The PyTRAF3IP1 cDNA is 2,367 bp, with an open reading frame of 1,629 bp encoding 542 amino acids. Phylogenetic and protein structural analysis confirmed the gene's identity and revealed that PyTRAF3IP1 was more similar to vertebrate TRAF3IP1s than to those of invertebrates. PyTRAF3IP1 was expressed in all the adult tissues and developmental stages sampled, implying that it plays versatile roles in many biological processes. Furthermore, PyTRAF3IP1 expression was dramatically induced in the acute phase (3-6 h) after infection with both Gram-positive (Micrococcus luteus) and Gram-negative (Vibrio anguillarum) bacteria, even stronger induction being observed after V. anguillarum challenge. This is the first report of the characterization and immune response involvement of TRAF3IP1 in marine invertebrates, and suggests that TRAF3IP1 contributes to innate immunity in bivalves.

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Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in microtubule stabilization

Cited by 87 publications

References 52 publications

The T cell IFT20 interactome reveals new players in immune synapse assembly

The T cell IFT20 interactome reveals new players in immune synapse assembly

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

Characterization of the <i>TRAF3IP1</i> gene in Yesso scallop (<i>Patinopecten yessoensis</i>) and its expression in response to bacterial challenge

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