Yang Niu,Cheng Zhang,Zhe Sun,Zhi Hong,Ke Li,Demeng Sun,Yanrui Yang,Changlin Tian,Weimin Gong & Jia-Jia Liu. PtdIns(4)P regulates retromerCmotor interaction to facilitate dyneinCcargo dissociation at the trans-Golgi network. Nature Cell Biology. DOI:10.1038/ncb2710 [分子发育生物学国家重点实验室]
<meta name="keywords" content="Yang Niu,Cheng Zhang,Zhe Sun,Zhi Hong,Ke Li,Demeng Sun,Yanrui Yang,Changlin Tian,Weimin Gong & Jia-Jia Liu. PtdIns(4)P regulates retromerCmotor interaction to facilitate dyneinCcargo dissociation at the trans-Golgi network. Nature Cell Biology. DOI:10.1038/ncb2710 ,YangNiu,ChengZhang,ZheSun,ZhiHong,KeLi,DemengSun,YanruiYang,ChanglinTian,WeiminGong&Jia-JiaLiuPtdIns4PregulatesretromerCmotorinteractiontofacilitatedyneinCcargodissociationatthetrans-GolginetworkNatureCellBiologyDOI:10103,分子发育生物学国家重点实验室">
<meta name="description" content="Yang Niu,Cheng Zhang,Zhe Sun,Zhi Hong,Ke Li,Demeng Sun,Yanrui Yang,Changlin Tian,Weimin Gong & Jia-Jia Liu. PtdIns(4)P regulates retromerCmotor interaction to facilitate dyneinCcargo dissociation at the trans-Golgi network. Nature Cell Biology. DOI:10.1038/ncb2710 [暂无简介]">
PtdIns(4)P regulates retromerCmotor interaction to facilitate dyneinCcargo dissociation at the trans-Golgi networkYang Niu,Cheng Zhang,Zhe Sun,Zhi Hong,Ke Li,Demeng Sun,Yanrui Yang,Changlin Tian,Weimin Gong & Jia-Jia LiuNature Cell Biology AbstractThe molecular mechanisms for the retrograde motor dyneinCdynactin to unload its cargoes at their final destination remain to be elucidated. In this study, we have investigated the regulatory mechanism underlying release of retromer-associated cargoes at the trans-Golgi network (TGN). We report that phosphotidylinositol-4-phosphate (PtdIns(4)P), a Golgi-enriched phosphoinositide, negatively regulates the proteinCprotein interaction between the p150Glued subunit of dyneinCdynactin and the retromer component SNX6. We show that PtdIns(4)P specifically facilitates dissociation of retromer-mediated membranous cargoes from the motor at the TGN and uncover an important function for PtdIns(4)P in the spatial control of retrograde vesicular trafficking to the TGN membrane. PtdIns(4)P also regulates SNX4-mediated retrograde vesicular trafficking to the endocytic recycling compartment by modulating its interaction with dynein. These results establish organelle-specific phosphoinositide regulation of motorCcargo interaction as a mechanism for cargo release by molecular motors at target membrane.扫扫二维码，随身浏览文档
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3秒自动关闭窗口Alzheimer-specific epitope of AT100 in transfected cell lines with ...
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1998 Oct 9;255(1):13-6.Alzheimer-specific epitope of AT100 in transfected cell lines with tau: toward an efficient cell model of tau abnormal phosphorylation.1, , , , .1INSERM U422, Lille, France.AbstractIntraneuronal aggregation of specific hyperphosphorylated tau isoforms in subsets of neurons may explain many neurodegenerative processes. Only some antibodies including AP422 and AT100 are specific to the abnormal phosphorylation of tau proteins in these processes. AT100-immunoreactivity was never observed in cell models with the exception of Sf9 cells. In the present study, we developed a way to induce AT100-immunoreactivity in different cell types including COS and SY5Y cells after tau cDNA transfection and treatment by okadaic acid. This represents a useful model to study abnormal tau phosphorylation in situ.PMID: 9839715
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External link. Please review our .Alzheimer-specific epitope of AT100 in transfected cell lines with ...
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FormatSummarySummary (text)AbstractAbstract (text)MEDLINEXMLPMID ListApplyChoose DestinationFileClipboardCollectionsE-mailOrderMy BibliographyCitation managerFormatSummary (text)Abstract (text)MEDLINEXMLPMID ListCSVCreate File1 selected item: 9839715FormatSummarySummary (text)AbstractAbstract (text)MEDLINEXMLPMID ListMeSH and Other DataE-mailSubjectAdditional textE-mailAdd to ClipboardAdd to CollectionsOrder articlesAdd to My BibliographyGenerate a file for use with external citation management software.Create File
1998 Oct 9;255(1):13-6.Alzheimer-specific epitope of AT100 in transfected cell lines with tau: toward an efficient cell model of tau abnormal phosphorylation.1, , , , .1INSERM U422, Lille, France.AbstractIntraneuronal aggregation of specific hyperphosphorylated tau isoforms in subsets of neurons may explain many neurodegenerative processes. Only some antibodies including AP422 and AT100 are specific to the abnormal phosphorylation of tau proteins in these processes. AT100-immunoreactivity was never observed in cell models with the exception of Sf9 cells. In the present study, we developed a way to induce AT100-immunoreactivity in different cell types including COS and SY5Y cells after tau cDNA transfection and treatment by okadaic acid. This represents a useful model to study abnormal tau phosphorylation in situ.PMID: 9839715
[PubMed - indexed for MEDLINE]
Publication TypesMeSH TermsSubstancesFull Text SourcesOther Literature SourcesMedicalMolecular Biology Databases
Supplemental Content
External link. Please review our .}