A role for novel lipid interactions in the dynamic recruitment of SNX27 to the T-cell immune synapse.
作者： María Tello-Lafoz , Rajesh Ghai , Brett Collins , Isabel Mérida
DOI: 10.1080/19490992.2015.1031950
关键词:
摘要: SNX27 is a member of the sorting nexin family that plays an important role in recycling receptors from endosomes to cell surface. In addition PX (Phox homology) domain regulates its endosomal localization, has unique PDZ (Psd-95/Dlg/ZO1) and atypical FERM (4.1, ezrin, radixin, moesin) both function bind short peptide sequence motifs cytoplasmic domains cargo receptors. Using T immune synapse (IS) as model for polarized protein recycling, we recently identified additional mechanism enhances localization compartment (ERC). Our study defined phosphoinositide (PI) lipid-binding site within domain, with clear preference bi- triphosphorylated PIs, which may promote phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and/or PtdIns(3,4,5)P3-enriched membrane domains. fluorescently tagged probes, studied kinetics distinct PIs living cells during IS formation. results suggest PtdIns(3,4,5)P3 accumulates at contact simultaneously early recruitment plasma (PM), this partly controlled by lipid binding through domain. These studies define 2 independent sites PtdIns-derived lipids SNX27, contribute dynamic membranes activation.
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