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10.1038/ncomms10777 http://scihub22266oqcxt.onion/10.1038/ncomms10777 C4773430!4773430 !26916822     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26916822 &cmd=llinks): Failed to open stream: HTTP request failed! 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Phosphatidylinositol phosphate kinase PIPKI? and phosphatase INPP5E coordinate initiation of ciliogenesis |pdf=|usr=}}{{26916822 }} gab.com Text Phosphatidylinositol phosphate kinase PIPKI and phosphatase INPP5E coordinate initiation of ciliogenesis JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26916822 #FOAvip Defective primary cilia are causative to a wide spectrum of human genetic disorders, termed ciliopathies. Although the regulation of ciliogenesis is intensively studied, how it is initiated remains unclear. Here we show that type I? phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinase (PIPKI?) and inositol polyphosphate-5-phosphatase E (INPP5E), a Joubert syndrome protein, localize to the centrosome and coordinate the initiation of ciliogenesis. PIPKI? counteracts INPP5E in regulating tau-tubulin kinase-2 (TTBK2) recruitment to the basal body, which promotes the removal of microtubule capping protein CP110 and the subsequent axoneme elongation. Interestingly, INPP5E and its product--PtdIns(4)P--accumulate at the centrosome/basal body in non-ciliated, but not ciliated, cells. PtdIns(4)P binding to TTBK2 and the distal appendage protein CEP164 compromises the TTBK2-CEP164 interaction and inhibits the recruitment of TTBK2. Our results reveal that PtdIns(4)P homoeostasis, coordinated by PIPKI? and INPP5E at the centrosome/ciliary base, is vital for ciliogenesis by regulating the CEP164-dependent recruitment of TTBK2. Twit Text FOAVip Phosphatidylinositol phosphate kinase PIPKI and phosphatase INPP5E coordinate initiation of ciliogenesis ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26916822 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26916822 #FOAvip English Wikipedia <ref>{{Cite pmid|26916822 }}</ref> Phosphatidylinositol phosphate kinase PIPKI? and phosphatase INPP5E coordinate initiation of ciliogenesis #MMPMID26916822 Xu Q ; Zhang Y ; Wei Q ; Huang Y ; Hu J ; Ling K Nat Commun 2016[Feb]; 7 (ä): 10777 PMID26916822 show ga Defective primary cilia are causative to a wide spectrum of human genetic disorders, termed ciliopathies. Although the regulation of ciliogenesis is intensively studied, how it is initiated remains unclear. Here we show that type I? phosphatidylinositol 4-phosphate (PtdIns(4)P) 5-kinase (PIPKI?) and inositol polyphosphate-5-phosphatase E (INPP5E), a Joubert syndrome protein, localize to the centrosome and coordinate the initiation of ciliogenesis. PIPKI? counteracts INPP5E in regulating tau-tubulin kinase-2 (TTBK2) recruitment to the basal body, which promotes the removal of microtubule capping protein CP110 and the subsequent axoneme elongation. Interestingly, INPP5E and its product--PtdIns(4)P--accumulate at the centrosome/basal body in non-ciliated, but not ciliated, cells. PtdIns(4)P binding to TTBK2 and the distal appendage protein CEP164 compromises the TTBK2-CEP164 interaction and inhibits the recruitment of TTBK2. Our results reveal that PtdIns(4)P homoeostasis, coordinated by PIPKI? and INPP5E at the centrosome/ciliary base, is vital for ciliogenesis by regulating the CEP164-dependent recruitment of TTBK2. |Animals [MESH] |Centrosome/*metabolism [MESH] |Cilia/*metabolism/ultrastructure [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Immunoprecipitation [MESH] |Mice [MESH] |Microscopy, Electron, Scanning [MESH] |Microscopy, Electron, Transmission [MESH] |Microscopy, Fluorescence [MESH] |Morphogenesis/*genetics [MESH] |NIH 3T3 Cells [MESH] |Phosphoric Monoester Hydrolases/*genetics/metabolism [MESH] |Phosphotransferases (Alcohol Group Acceptor)/*genetics [MESH]Phosphatidylinositol phosphate kinase PIPKI? and phosphatase INPP5E co(epmc).pdf DeepDyve Pubget Overpricing