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Although Hrs acts as a key transporter for ubiquitin-dependent endosomal sorting, we previously reported that Hrs is also involved in ubiquitin-independent endosomal sorting of interleukin-2 receptor beta (IL-2R beta). Here, we show direct interactions between bacterially expressed Hrs and interleukin-4 receptor alpha (IL-4R alpha), indicating that their binding is not required for ubiquitylation of the receptors, similar to the case for IL-2R beta. Examinations of the Hrs binding regions of the receptors reveal that a hydrophobic amino acid cluster in both IL-2R beta and IL-4R alpha is essential for the binding. Whereas the wild-type receptors are delivered to LAMP1-positive late endosomes, mutant receptors lacking the hydrophobic amino acid cluster are sorted to lysobisphosphatidic acid-positive late endosomes rather than LAMP1-positive late endosomes. We also show that the degradation of these mutant receptors is attenuated. 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Amano Y, et al. Hrs Recognizes a Hydrophobic Amino Acid Cluster in Cytokine Receptors during Ubiquitin-independent Endosomal Sorting. The Journal of Biological Chemistry. 2011; 286:15458-15472. \u00a9 the American Society for Biochemistry and Molecular Biology."}]}, "item_6_select_64": {"attribute_name": "\u8457\u8005\u7248\u30d5\u30e9\u30b0", "attribute_value_mlt": [{"subitem_select_item": "author"}]}, "item_6_source_id_35": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0021-9258", "subitem_source_identifier_type": "PISSN"}]}, "item_6_source_id_39": {"attribute_name": "NII ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0021-9258", "subitem_source_identifier_type": "PISSN"}]}, "item_6_source_id_40": {"attribute_name": "\u66f8\u8a8c\u30ec\u30b3\u30fc\u30c9ID", "attribute_value_mlt": [{"subitem_source_identifier": "AA00251083", "subitem_source_identifier_type": "NCID"}]}, "item_6_text_70": {"attribute_name": "wosonly keywords", "attribute_value_mlt": [{"subitem_text_value": "TRANSDUCING ADAPTER MOLECULE; HUMAN IL-2 RECEPTOR; FACTOR-II RECEPTOR; ESCRT-III; PLASMA-MEMBRANE; GAMMA-CHAIN; TYROSINE PHOSPHORYLATION; RAPID INTERNALIZATION; MONOCLONAL-ANTIBODIES; CYTOPLASMIC TAIL"}]}, "item_6_textarea_68": {"attribute_name": "wosonly abstract", "attribute_value_mlt": [{"subitem_textarea_value": "Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) is a component of the ESCRT-0 protein complex that captures ubiquitylated cargo proteins and sorts them to the lysosomal pathway. Although Hrs acts as a key transporter for ubiquitin-dependent endosomal sorting, we previously reported that Hrs is also involved in ubiquitin-independent endosomal sorting of interleukin-2 receptor beta (IL-2R beta). Here, we show direct interactions between bacterially expressed Hrs and interleukin-4 receptor alpha (IL-4R alpha), indicating that their binding is not required for ubiquitylation of the receptors, similar to the case for IL-2R beta. Examinations of the Hrs binding regions of the receptors reveal that a hydrophobic amino acid cluster in both IL-2R beta and IL-4R alpha is essential for the binding. Whereas the wild-type receptors are delivered to LAMP1-positive late endosomes, mutant receptors lacking the hydrophobic amino acid cluster are sorted to lysobisphosphatidic acid-positive late endosomes rather than LAMP1-positive late endosomes. We also show that the degradation of these mutant receptors is attenuated. 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