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Acid Sphingomyelinase regulates the localization and trafficking of palmitoylated proteins.

Biol Open. 2019; 
XiongXiahui,LeeChia-Fang,LiWenjing,YuJiekai,ZhuLinyu,KimYongsoon,ZhangHui,Sun
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Mutagenesis Services 1-N-eGFP vector to derive the pcDNA-N-GFP-SNAP23 construct (service provided by GenScript, Piscataway, NJ).... Site-directed mutagenesis of SNAP23 and Lyn to introduce Cys->Ser mutations were conducted by GenScript (Piscataway, NJ) and all cDNAs were confirmed by sequencing. Get A Quote

摘要

In human, loss of Acid Sphingomeylinase (ASM/SMPD1) causes Niemann-Pick Disease, type A. ASM hydrolyzes sphingomyelins to produce ceramides but protein targets of ASM remain largely unclear. Our mass-spectrometry-based proteomic analyses have identified >100 proteins associated with the ASM-dependent, detergent-resistant membrane microdomains (lipid rafts), with >60% of these proteins being palmitoylated, including SNAP23, Src-family kinases Yes and Lyn, and Ras and Rab family small GTPases. Inactivation of ASM abolished the presence of these proteins in the plasma membrane, with many of them trapped in the Golgi. While palmitoylation inhibitors and palmitoylation mutants phenocopied the effects... More

关键词

Acid sphingomyelinase,Ceramide,Golgi,Lipid raft,Plasma membrane,Protein palmitoylation,Protein trafficking,Proteo