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10.1038/ncomms10777 http://scihub22266oqcxt.onion/10.1038/ncomms10777 C4773430!4773430!26916822     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2016 ; 7 (ä): ä Nephropedia Template TP {{tp|p=26916822|t=2016. 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[]; 7 (ä): ä PMID26916822show 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. äPhosphatidylinositol phosphate kinase PIPKI? and phosphatase INPP5E co(epmc).pdf DeepDyve Pubget Overpricing