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10.15252/embj.201593148 http://scihub22266oqcxt.onion/10.15252/embj.201593148 C5007553!5007553 !27340123     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27340123 &cmd=llinks): Failed to open stream: HTTP request failed! 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Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome |pdf=|usr=}}{{27340123 }} gab.com Text Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=27340123 #FOAvip Autophagy is a multistep membrane traffic pathway. In contrast to autophagosome formation, the mechanisms underlying autophagosome-lysosome fusion remain largely unknown. Here, we describe a novel autophagy regulator, inositol polyphosphate-5-phosphatase E (INPP5E), involved in autophagosome-lysosome fusion process. In neuronal cells, INPP5E knockdown strongly inhibited autophagy by impairing the fusion step. A fraction of INPP5E is localized to lysosomes, and its membrane anchoring and enzymatic activity are necessary for autophagy. INPP5E decreases lysosomal phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2), one of the substrates of the phosphatase, that counteracts cortactin-mediated actin filament stabilization on lysosomes. Lysosomes require actin filaments on their surface for fusing with autophagosomes. INPP5E is one of the genes responsible for Joubert syndrome, a rare brain abnormality, and mutations found in patients with this disease caused defects in autophagy. Taken together, our data reveal a novel role of phosphoinositide on lysosomes and an association between autophagy and neuronal disease. Twit Text FOAVip Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=27340123 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27340123 #FOAvip English Wikipedia <ref>{{Cite pmid|27340123 }}</ref> Autophagosome-lysosome fusion in neurons requires INPP5E, a protein associated with Joubert syndrome #MMPMID27340123 Hasegawa J ; Iwamoto R ; Otomo T ; Nezu A ; Hamasaki M ; Yoshimori T EMBO J 2016[Sep]; 35 (17 ): 1853-67 PMID27340123 show ga Autophagy is a multistep membrane traffic pathway. In contrast to autophagosome formation, the mechanisms underlying autophagosome-lysosome fusion remain largely unknown. Here, we describe a novel autophagy regulator, inositol polyphosphate-5-phosphatase E (INPP5E), involved in autophagosome-lysosome fusion process. In neuronal cells, INPP5E knockdown strongly inhibited autophagy by impairing the fusion step. A fraction of INPP5E is localized to lysosomes, and its membrane anchoring and enzymatic activity are necessary for autophagy. INPP5E decreases lysosomal phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2), one of the substrates of the phosphatase, that counteracts cortactin-mediated actin filament stabilization on lysosomes. Lysosomes require actin filaments on their surface for fusing with autophagosomes. INPP5E is one of the genes responsible for Joubert syndrome, a rare brain abnormality, and mutations found in patients with this disease caused defects in autophagy. Taken together, our data reveal a novel role of phosphoinositide on lysosomes and an association between autophagy and neuronal disease. |*Membrane Fusion [MESH] |Abnormalities, Multiple/pathology [MESH] |Autophagosomes/*metabolism [MESH] |Cerebellum/abnormalities/pathology [MESH] |Eye Abnormalities/pathology [MESH] |Humans [MESH] |Kidney Diseases, Cystic/pathology [MESH] |Lysosomes/*metabolism [MESH] |Neurons/*physiology [MESH] |Phosphoric Monoester Hydrolases/*metabolism [MESH]Autophagosome-lysosome fusion in neurons requires INPP5E, a protein as(epmc).pdf DeepDyve Pubget Overpricing