Intraflagellar transport complex structure and cargo interactions - PubMed (original) (raw)

Intraflagellar transport complex structure and cargo interactions

Sagar Bhogaraju et al. Cilia. 2013.

Abstract

Intraflagellar transport (IFT) is required for the assembly and maintenance of cilia, as well as the proper function of ciliary motility and signaling. IFT is powered by molecular motors that move along the axonemal microtubules, carrying large complexes of IFT proteins that travel together as so-called trains. IFT complexes likely function as adaptors that mediate interactions between anterograde/retrograde motors and ciliary cargoes, facilitating cargo transport between the base and tip of the cilium. Here, we provide an up-to-date review of IFT complex structure and architecture, and discuss how interactions with cargoes and motors may be achieved.

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Figures

Figure 1

Figure 1

Domain organization and known cargo interactions of intraflagellar transport complex proteins. Intraflagellar transport (IFT) proteins are divided into distinct modules, referred to in this review as principal domains (PDs) and auxiliary domains (ADs), serving principal structural (blue) and auxiliary interaction (red) roles, respectively. Proteins for which there may not be a clear boundary between PD and AD are labeled as “PD/AD”. The probable interacting cargoes of various IFT ADs are indicated with a dashed line. The ADs of IFT81, IFT74, IFT52, IFT54 and IFT57 still remain to be characterized. All of the IFT proteins are abbreviated as the numerical part of their names. The letters N, M and C next to the numbers refer to the N-terminal, middle and C-terminal domains of the corresponding protein. IFT-A proteins, IFT80 and IFT22 are colored grey because their associations with other IFT proteins and ciliary cargoes are poorly characterized. EB1, End binding protein 1; GPCR, G-protein coupled receptor; MRJ, Mammalian relative of DNAJ; ODA, outer dynein arms; OSM, Osmotic avoidance abnormal protein; Ttll6, Tubulin tyrosine ligase-like 6; TULP3, tubby like protein 3.

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