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10.1091/mbc.E16-01-0040 http://scihub22266oqcxt.onion/10.1091/mbc.E16-01-0040 C4831875!4831875 !26912790     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26912790 &cmd=llinks): Failed to open stream: HTTP request failed! 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A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia |pdf=|usr=}}{{26912790 }} gab.com Text A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia JO: Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26912790 #FOAvip WDR92 is a highly conserved WD-repeat protein that has been proposed to be involved in apoptosis and also to be part of a prefoldin-like cochaperone complex. We found that WDR92 has a phylogenetic signature that is generally compatible with it playing a role in the assembly or function of specifically motile cilia. To test this hypothesis, we performed an RNAi-based knockdown of WDR92 gene expression in the planarianSchmidtea mediterraneaand were able to achieve a robust reduction in mRNA expression to levels undetectable under our standard RT-PCR conditions. We found that this treatment resulted in a dramatic reduction in the rate of organismal movement that was caused by a switch in the mode of locomotion from smooth, cilia-driven gliding to muscle-based, peristaltic contractions. Although the knockdown animals still assembled cilia of normal length and in similar numbers to controls, these structures had reduced beat frequency and did not maintain hydrodynamic coupling. By transmission electron microscopy we observed that many cilia had pleiomorphic defects in their architecture, including partial loss of dynein arms, incomplete closure of the B-tubule, and occlusion or replacement of the central pair complex by accumulated electron-dense material. These observations suggest that WDR92 is part of a previously unrecognized cytoplasmic chaperone system that is specifically required to fold key components necessary to build motile ciliary axonemes. Twit Text FOAVip A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia ????Mol Biol Cell http://www.kidney.de/pget.php?&tw=1&pmid=26912790 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26912790 #FOAvip English Wikipedia <ref>{{Cite pmid|26912790 }}</ref> A prefoldin-associated WD-repeat protein (WDR92) is required for the correct architectural assembly of motile cilia #MMPMID26912790 Patel-King RS ; King SM Mol Biol Cell 2016[Apr]; 27 (8 ): 1204-9 PMID26912790 show ga WDR92 is a highly conserved WD-repeat protein that has been proposed to be involved in apoptosis and also to be part of a prefoldin-like cochaperone complex. We found that WDR92 has a phylogenetic signature that is generally compatible with it playing a role in the assembly or function of specifically motile cilia. To test this hypothesis, we performed an RNAi-based knockdown of WDR92 gene expression in the planarianSchmidtea mediterraneaand were able to achieve a robust reduction in mRNA expression to levels undetectable under our standard RT-PCR conditions. We found that this treatment resulted in a dramatic reduction in the rate of organismal movement that was caused by a switch in the mode of locomotion from smooth, cilia-driven gliding to muscle-based, peristaltic contractions. Although the knockdown animals still assembled cilia of normal length and in similar numbers to controls, these structures had reduced beat frequency and did not maintain hydrodynamic coupling. By transmission electron microscopy we observed that many cilia had pleiomorphic defects in their architecture, including partial loss of dynein arms, incomplete closure of the B-tubule, and occlusion or replacement of the central pair complex by accumulated electron-dense material. These observations suggest that WDR92 is part of a previously unrecognized cytoplasmic chaperone system that is specifically required to fold key components necessary to build motile ciliary axonemes. |Animals [MESH] |Axoneme/metabolism [MESH] |Cilia/genetics/metabolism/ultrastructure [MESH] |Gene Knockdown Techniques [MESH] |Helminth Proteins/*chemistry/genetics/*metabolism [MESH] |Microscopy, Electron, Transmission [MESH] |Molecular Chaperones/metabolism [MESH] |Multiprotein Complexes/metabolism [MESH] |Phylogeny [MESH] |Planarians/*cytology/genetics/metabolism [MESH]A prefoldin-associated WD-repeat protein (WDR92) is required for the c(epmc).pdf DeepDyve Pubget Overpricing