{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["29(22)"],"submitter":["Zhang J"],"pubmed_abstract":["Stabilin-1 is a unique scavenger receptor that combines endocytic and intracellular sorting functions in macrophages. Stabilin-1 mediates the endocytosis of acetylated low-density lipoprotein (acLDL), SPARC, and growth hormone family member placental lactogen (PL). At the same time, stabilin-1 is involved in trans-Golgi network-to-endosome routing of the endogenous chitinase-like protein SI-CLP (stabilin-interacting chitinase-like protein). A DDSLL motif in the cytoplasmic tail of stabilin-1 interacts with GGA adaptors; however, the deletion of DDSLL reduces but does not abrogate this interaction. Here, we identified a novel GGA-binding site, EDDADDD, in the cytoplasmic tail of stabilin-1. The deletion of EDDADDD impaired and the deletion of both the DDSLL and EDDADDD sites abrogated the i"],"journal":["Molecular and cellular biology"],"pagination":["6097-105"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2772567"],"repository":["biostudies-literature"],"pubmed_title":["A novel GGA-binding site is required for intracellular sorting mediated by stabilin-1."],"pmcid":["PMC2772567"],"pubmed_authors":["Gratchev A","Sage EH","Schmuttermaier C","Zhang J","Mamidi S","Krusell L","Kremmer E","Kzhyshkowska J","Riabov V","Jalkanen S","Workman G","Goerdt S"],"additional_accession":[]},"is_claimable":false,"name":"A novel GGA-binding site is required for intracellular sorting mediated by stabilin-1.","description":"Stabilin-1 is a unique scavenger receptor that combines endocytic and intracellular sorting functions in macrophages. Stabilin-1 mediates the endocytosis of acetylated low-density lipoprotein (acLDL), SPARC, and growth hormone family member placental lactogen (PL). At the same time, stabilin-1 is involved in trans-Golgi network-to-endosome routing of the endogenous chitinase-like protein SI-CLP (stabilin-interacting chitinase-like protein). A DDSLL motif in the cytoplasmic tail of stabilin-1 interacts with GGA adaptors; however, the deletion of DDSLL reduces but does not abrogate this interaction. Here, we identified a novel GGA-binding site, EDDADDD, in the cytoplasmic tail of stabilin-1. The deletion of EDDADDD impaired and the deletion of both the DDSLL and EDDADDD sites abrogated the i","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Nov","modification":"2025-04-18T15:07:44.289Z","creation":"2019-03-27T00:26:21Z"},"accession":"S-EPMC2772567","cross_references":{"pubmed":["19752197"],"doi":["10.1128/mcb.00505-09","10.1128/MCB.00505-09"]}}