Search results for TTC26

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Protein (2 results from a total of 2)

Identifier: R-HSA-5637963
Species: Homo sapiens
Compartment: cilium
Primary external reference: UniProt: TTC26: A0AVF1
Identifier: R-HSA-5637962
Species: Homo sapiens
Compartment: ciliary tip
Primary external reference: UniProt: TTC26: A0AVF1

Reaction (2 results from a total of 2)

Identifier: R-HSA-5625416
Species: Homo sapiens
Compartment: cilium
Anterograde trains travel along the axoneme of the cilium at an estimated rate of 2 micrometers per second in an ATP- and kinesin-2-dependent fashion (reviewed in Cole and Snell, 2009). Although the particulars of IFT train-cargo interactions have not been fully elaborated, recent studies in C. reinhardtii and human cells have shown that the IFT B components IFT74 and IFT81 have tubulin-binding sites, while IFT46 is required for the ciliary transport of the outer dynein arm, and more recently, TTC26 has been shown to be required for the transport of motility-related proteins into the flagella (Bhogaraju et al, 2013; Ahmed et al, 2008; Hou et al, 2007; Ishikawa et al, 2014; reviewed in Bhogarju et al, 2014).
Identifier: R-HSA-5617820
Species: Homo sapiens
Compartment: cilium
Based on studies done in C. reinhardtii, C. elegans and mouse, the human IFT B complex likely consists of, minimally, IFT20, RABL5/IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT74, IFT80, IFT81, IFT88, CLUAP/QILIN, IFT70/TTC30, and TTC26/IFT56, with IFT172 being an additional candidate (Follit et al, 2009; Piperno and Mead, 1997; Cole et al, 1998; Cole, 2003; Ou, 2007; Hallbritter et al, 2013; reviewed in Taschner et al, 2012). Work in C. reinhardtii and mouse suggests that IFT B consists of a salt stable core complex of IFT88, IFT81, IFT74, IFT70, IFT52, IFT46 IFT 27, IFT25 and IFT22 with peripheral, weakly associated subunits IFT 172, IFT80, IFT57, CLUAP, TTC26 and IFT20 (Lucker et al, 2005; Lucker et al, 2010; Follit et al, 2009; Bhogaraju et al, 2011). In Chlamydomonas, core components IFT81 and IFT74 have been shown to interact directly and a stable sub-complex of IFT81/74/27/25 has been demonstrated (Lucker et al, 2005; Taschner et al, 2011). Human IFT81 and IFT74 have likewise been shown to directly interact and to form a tubulin-binding complex (Bhogaraju et al, 2013). A recent study has elucidated more detail of the protein-protein interactions that direct the assembly of the IFTB complex (Taschner et al, 2014).
This reaction shows putative human IFT B proteins assembling in a single step; details of how and when this assembly occurs are not shown, nor are the specific protein-protein interactions within the complex or details of how IFT B is regulated. Moreover, this reaction shows the formation of a presumptive IFT B* complex, lacking IFT20, to allow the recruitment of IFT20 from the Golgi compartment to be depicted.
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