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http://purl.uniprot.org/citations/37802024http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37802024http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37802024http://www.w3.org/2000/01/rdf-schema#comment"p62 is a well-characterized autophagy receptor that recognizes and sequesters specific cargoes into autophagosomes for degradation. p62 promotes the assembly and removal of ubiquitinated proteins by forming p62-liquid droplets. However, it remains unclear how autophagosomes efficiently sequester p62 droplets. Herein, we report that p62 undergoes reversible S-acylation in multiple human-, rat-, and mouse-derived cell lines, catalyzed by zinc-finger Asp-His-His-Cys S-acyltransferase 19 (ZDHHC19) and deacylated by acyl protein thioesterase 1 (APT1). S-acylation of p62 enhances the affinity of p62 for microtubule-associated protein 1 light chain 3 (LC3)-positive membranes and promotes autophagic membrane localization of p62 droplets, thereby leading to the production of small LC3-positive p62 droplets and efficient autophagic degradation of p62-cargo complexes. Specifically, increasing p62 acylation by upregulating ZDHHC19 or by genetic knockout of APT1 accelerates p62 degradation and p62-mediated autophagic clearance of ubiquitinated proteins. Thus, the protein S-acylation-deacylation cycle regulates p62 droplet recruitment to the autophagic membrane and selective autophagic flux, thereby contributing to the control of selective autophagic clearance of ubiquitinated proteins."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2023.09.004"xsd:string
http://purl.uniprot.org/citations/37802024http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2023.09.004"xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Chen X."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Huang X."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Huang X."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Ouyang S."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Ouyang S."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Neculai D."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Neculai D."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Luo D."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Luo D."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Sun Q."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Sun Q."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Lin C."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Lin C."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/37802024http://purl.uniprot.org/core/author"Wang Z."xsd:string