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- W2084080258 abstract "Endosomal trafficking and degradation of epidermal growth factor receptor (EGFR) play an essential role in the control of its signaling. Phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P2) is an established regulator of endocytosis, whereas PtdIns3P modulates endosomal trafficking. However, we demonstrate here that type I gamma phosphatidylinositol phosphate 5-kinase i5 (PIPKIγi5), an enzyme that synthesizes PtdIns4,5P2, controls endosome-to-lysosome sorting of EGFR. In this pathway, PIPKIγi5 interacts with sorting nexin 5 (SNX5), a protein that binds PtdIns4,5P2 and other phosphoinositides. PIPKIγi5 and SNX5 localize to endosomes, and loss of either protein blocks EGFR sorting into intraluminal vesicles (ILVs) of the multivesicular body. Loss of ILV sorting greatly enhances and prolongs EGFR signaling. PIPKIγi5 and SNX5 prevent Hrs ubiquitination, and this facilitates the Hrs association with EGFR that is required for ILV sorting. These findings reveal that PIPKIγi5 and SNX5 form a signaling nexus that controls EGFR endosomal sorting, degradation, and signaling." @default.
- W2084080258 created "2016-06-24" @default.
- W2084080258 creator A5017586422 @default.
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- W2084080258 creator A5055281869 @default.
- W2084080258 creator A5059181659 @default.
- W2084080258 creator A5083589251 @default.
- W2084080258 date "2013-04-01" @default.
- W2084080258 modified "2023-10-07" @default.
- W2084080258 title "Endosomal Type Iγ PIP 5-Kinase Controls EGF Receptor Lysosomal Sorting" @default.
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- W2084080258 doi "https://doi.org/10.1016/j.devcel.2013.03.010" @default.
- W2084080258 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3740164" @default.
- W2084080258 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23602387" @default.
- W2084080258 hasPublicationYear "2013" @default.
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