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• W2151184795 abstract "Mutation of the inositol polyphosphate 5-phosphatase OCRL1 results in two disorders in humans, namely Lowe syndrome (characterized by ocular, nervous system, and renal defects) and type 2 Dent disease (in which only the renal symptoms are evident). The disease mechanisms of these syndromes are poorly understood. Here we identify two novel OCRL1-binding proteins, termed inositol polyphosphate phosphatase interacting protein of 27 kDa (IPIP27)A and B (also known as Ses1 and 2), that also bind the related 5-phosphatase Inpp5b. The IPIPs bind to the C-terminal region of these phosphatases via a conserved motif similar to that found in the signaling protein APPL1. IPIP27A and B, which form homo- and heterodimers, localize to early and recycling endosomes and the trans-Golgi network (TGN). The IPIPs are required for receptor recycling from endosomes, both to the TGN and to the plasma membrane. Our results identify IPIP27A and B as key players in endocytic trafficking and strongly suggest that defects in this process are responsible for the pathology of Lowe syndrome and Dent disease." @default.
• W2151184795 created "2016-06-24" @default.
• W2151184795 creator A5010533721 @default.
• W2151184795 creator A5048387889 @default.
• W2151184795 creator A5052587383 @default.
• W2151184795 date "2011-03-01" @default.
• W2151184795 modified "2023-10-14" @default.
• W2151184795 title "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway" @default.
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• W2151184795 doi "https://doi.org/10.1091/mbc.e10-08-0730" @default.
• W2151184795 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3046058" @default.
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• W2151184795 hasPublicationYear "2011" @default.
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