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

Taschner, M., Weber, K., Mourao, A., Vetter, M., Awasthi, M., Stiegler, M., et al. (2016). Intraflagellar transport proteins 172, 80, 57, 54, 38, and 20 form a stable tubulin-binding IFT-B2 complex. EMBO JOURNAL, 35(7), 773-790. doi:10.15252/embj.201593164.

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 Creators:
Taschner, Michael1, Author              
Weber, Kristina1, Author              
Mourao, Andre1, Author              
Vetter, Melanie1, Author              
Awasthi, Mayanka1, Author              
Stiegler, Marc1, Author              
Bhogaraju, Sagar1, Author              
Lorentzen, Esben1, Author              
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1Lorentzen, Esben / Intraflagellar Transport, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565157              

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Free keywords: CAENORHABDITIS-ELEGANS; SENSORY CILIA; B CORE; FUNCTIONAL-ANALYSIS; CYTOPLASMIC DYNEIN; FLAGELLAR PROTEINS; PROTEOMIC ANALYSIS; CRYSTAL-STRUCTURE; KIDNEY-DISEASE; CYSTIC KIDNEYcilia; IFT54; IFT-B; intraflagellar transport; tubulin transpor;
 Abstract: 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-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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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000373714300008
DOI: 10.15252/embj.201593164
 Degree: -

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Title: EMBO JOURNAL
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY-BLACKWELL
Pages: - Volume / Issue: 35 (7) Sequence Number: - Start / End Page: 773 - 790 Identifier: ISSN: 0261-4189