| Structural highlights
Function
MIPT3_HUMAN Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules.[1] [2] [3]
Publication Abstract from PubMed
The intraflagellar transport (IFT) machinery plays a crucial role in the bidirectional trafficking of components necessary for ciliary signaling, such as the Hedgehog, Wnt/PCR, and cAMP/PKA systems. Defects in some components of the IFT machinery cause dysfunction, leading to a wide range of human diseases and developmental disorders termed ciliopathies, such as nephronophthisis. The IFT machinery comprises three sub-complexes: BBsome, IFT-A, and IFT-B. The IFT protein 54 (IFT54) is an important component of the IFT-B sub-complex. In anterograde movement, IFT54 binds to active kinesin-II, walking along the cilia microtubule axoneme and carrying the dynein-2 complex in an inactive state, which works for retrograde movement. Several mutations in IFT54 are known to cause Senior-Loken syndrome, a ciliopathy. IFT54 possesses a divergent Calponin Homology (CH) domain termed as NN-CH domain at its N-terminus. However, several aspects of the function of the NN-CH domain of IFT54 are still obscure. Here, we report the (1)H, (15)N, and (13)C resonance assignments of the NN-CH domain of human IFT54 and its solution structure. The NN-CH domain of human IFT54 adopts essentially the alpha1-alpha2-alpha3-alpha4-alpha5 topology as that of mouse IFT54, whose structure was determined by X-ray crystallographic study. The structural information and assignments obtained in this study shed light on the molecular function of the NN-CH domain in IFT54.
(1)H, (13)C, and (15)N resonance assignments and solution structure of the N-terminal divergent calponin homology (NN-CH) domain of human intraflagellar transport protein 54.,Kuwasako K, Dang W, He F, Takahashi M, Tsuda K, Nagata T, Tanaka A, Kobayashi N, Kigawa T, Guntert P, Shirouzu M, Yokoyama S, Muto Y Biomol NMR Assign. 2024 Jun;18(1):71-78. doi: 10.1007/s12104-024-10170-w. Epub , 2024 Mar 29. PMID:38551798[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ling L, Goeddel DV. MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network. J Biol Chem. 2000 Aug 4;275(31):23852-60. PMID:10791955 doi:http://dx.doi.org/10.1074/jbc.M001095200
- ↑ Niu Y, Murata T, Watanabe K, Kawakami K, Yoshimura A, Inoue J, Puri RK, Kobayashi N. MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation. FEBS Lett. 2003 Aug 28;550(1-3):139-43. PMID:12935900
- ↑ Morris JA, Kandpal G, Ma L, Austin CP. DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Hum Mol Genet. 2003 Jul 1;12(13):1591-608. PMID:12812986
- ↑ Kuwasako K, Dang W, He F, Takahashi M, Tsuda K, Nagata T, Tanaka A, Kobayashi N, Kigawa T, Güntert P, Shirouzu M, Yokoyama S, Muto Y. (1)H, (13)C, and (15)N resonance assignments and solution structure of the N-terminal divergent calponin homology (NN-CH) domain of human intraflagellar transport protein 54. Biomol NMR Assign. 2024 Jun;18(1):71-78. PMID:38551798 doi:10.1007/s12104-024-10170-w
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