The IFT A complex is believed to be composed of six components: WDR19/IFT144, IFT140, IFT122, TTC21B/IFT139, WDR35/IFT121 and IFT43 (Piperno et al, 1998; Cole and Snell, 2009; reviewed in Taschner et al, 2012). Each of these proteins was identified as a TULP3-interacting protein in human cells, supporting the notion established in other organisms that they are all components of the IFT A complex (Mukhopadhyay et al, 2010; reviewed in Taschner et al, 2012). The IFT A proteins are large and generally have similar domain organization, consisting of N-terminal WD motifs and C-terminal TPR repeats. These protein interaction domains may help the IFT A complex scaffold recruitment of the IFT B complex, as well as recruit ciliary cargo and motor proteins. Intriguingly, the domain structure of IFT A proteins is similar to that of nucleoporins and coat proteins and it has been suggested that they evolved from a coat protein precursor, consistent with a role in vesicle trafficking (Devos et al, 2004; Jekely and Arendt, 2006).Details of protein-protein interactions within the IFT A complex are not known, nor are the details of how and where the complex assembles in a human cell.
Chait, BT, Alber, F, Devos, D, Dokudovskaya, S, Williams, R, Rout, MP, Sali, A
Snell, WJ, Cole, DG
Piperno, G, Segil, M, Siuda, E, Vaananen, H, Henderson, S, Sassaroli, M
Lane, WS, Scales, SJ, Wen, X, Chih, B, Jackson, PK, Nelson, CD, Mukhopadhyay, S
Arendt, D, Jékely, G
Bhogaraju, S, Taschner, M, Lorentzen, E
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