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http://purl.uniprot.org/citations/31904398http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31904398http://www.w3.org/2000/01/rdf-schema#comment"RLIP (Ral-interacting protein) is a multifunctional protein that couples ATP hydrolysis with the movement of substances. Its primary function appears to be in the plasma membrane, where it catalyzes the ATP-dependent efflux of glutathione-conjugates (GS-Es), as well as un-metabolized drugs and toxins. In the plasma membrane, its interaction with the clathrin adaptor protein AP2 localizes it to endocytic vesicle, where its GS-E-stimulated ATPase and transport activity are required for clathrin-dependent endocytosis (CDE). CDE is an essential mechanism for internalizing ligand-receptor complexes that signal proliferation (EGF, insulin, IGF1), apoptosis (TNFα, TRAIL, Fas-L), and differentiation and morphogenesis (TGFβ, WNT, Notch, SHH). Aberrant functioning of these pathways appears crucial for most cancer cells to evade apoptosis, invade surrounding tissues, and metastasize. Internalization of receptor-ligand complexes by CDE begins a sequence of events that can terminate, initiate, or modulate downstream signaling; the consequences of signaling through these downstream pathways may be inherently different in cancer and normal cells, a view supported by numerous basic and clinical observations. In this review, we will discuss the GS-E transport activity of RLIP, which determines the rate of ligand endocytosis, and how the inhibition and/or depletion of RLIP globally disrupts in ligand-receptor signaling."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.org/dc/terms/identifier"doi:10.1016/j.bbcan.2020.188337"xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/author"Verma N."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/author"Awasthi S."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/author"Horne D."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/author"Salgia R."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/author"Singhal S.S."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/name"Biochim Biophys Acta Rev Cancer"xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/pages"188337"xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/title"RLIP controls receptor-ligand signaling by regulating clathrin-dependent endocytosis."xsd:string
http://purl.uniprot.org/citations/31904398http://purl.uniprot.org/core/volume"1873"xsd:string
http://purl.uniprot.org/citations/31904398http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31904398
http://purl.uniprot.org/citations/31904398http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31904398
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http://purl.uniprot.org/uniprot/#_Q15311-mappedCitation-31904398http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31904398
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http://purl.uniprot.org/uniprot/Q15311http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31904398
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