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10.1038/ncomms9205 http://scihub22266oqcxt.onion/10.1038/ncomms9205 C4570271!4570271 !26365782     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26365782 &cmd=llinks): Failed to open stream: HTTP request failed! 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Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled |pdf=|usr=}}{{26365782 }} gab.com Text Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26365782 #FOAvip Type I phosphatidylinositol phosphate kinase (PIP5K1) phosphorylates the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate PtdIns4,5P2, which plays important roles in a wide range of cellular functions including Wnt signalling. However, the lack of its structural information has hindered the understanding of its regulation. Here we report the crystal structure of the catalytic domain of zebrafish PIP5K1A at 3.3?Å resolution. This molecule forms a side-to-side dimer. Mutagenesis study of PIP5K1A reveals two adjacent interfaces for the dimerization and interaction with the DIX domain of the Wnt signalling molecule dishevelled. Although these interfaces are located distally to the catalytic/substrate-binding site, binding to these interfaces either through dimerization or the interaction with DIX stimulates PIP5K1 catalytic activity. DIX binding additionally enhances PIP5K1 substrate binding. Thus, this study elucidates regulatory mechanisms for this lipid kinase and provides a paradigm for the understanding of PIP5K1 regulation by their interacting molecules. Twit Text FOAVip Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26365782 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26365782 #FOAvip English Wikipedia <ref>{{Cite pmid|26365782 }}</ref> Resolution of structure of PIP5K1A reveals molecular mechanism for its regulation by dimerization and dishevelled #MMPMID26365782 Hu J ; Yuan Q ; Kang X ; Qin Y ; Li L ; Ha Y ; Wu D Nat Commun 2015[Sep]; 6 (ä): 8205 PMID26365782 show ga Type I phosphatidylinositol phosphate kinase (PIP5K1) phosphorylates the head group of phosphatidylinositol 4-phosphate (PtdIns4P) to generate PtdIns4,5P2, which plays important roles in a wide range of cellular functions including Wnt signalling. However, the lack of its structural information has hindered the understanding of its regulation. Here we report the crystal structure of the catalytic domain of zebrafish PIP5K1A at 3.3?Å resolution. This molecule forms a side-to-side dimer. Mutagenesis study of PIP5K1A reveals two adjacent interfaces for the dimerization and interaction with the DIX domain of the Wnt signalling molecule dishevelled. Although these interfaces are located distally to the catalytic/substrate-binding site, binding to these interfaces either through dimerization or the interaction with DIX stimulates PIP5K1 catalytic activity. DIX binding additionally enhances PIP5K1 substrate binding. Thus, this study elucidates regulatory mechanisms for this lipid kinase and provides a paradigm for the understanding of PIP5K1 regulation by their interacting molecules. |*Dimerization [MESH] |Adaptor Proteins, Signal Transducing/*metabolism [MESH] |Animals [MESH] |Binding Sites [MESH] |Calorimetry [MESH] |Catalytic Domain [MESH] |Circular Dichroism [MESH] |Crystallization [MESH] |Crystallography, X-Ray [MESH] |Dishevelled Proteins [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Phosphatidylinositol 4,5-Diphosphate/metabolism [MESH] |Phosphatidylinositol Phosphates/metabolism [MESH] |Phosphoproteins/*metabolism [MESH] |Phosphorylation [MESH] |Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism [MESH] |Protein Structure, Tertiary [MESH]Resolution of structure of PIP5K1A reveals molecular mechanism for its(epmc).pdf DeepDyve Pubget Overpricing