Hrs Recognizes a Hydrophobic Amino Acid Cluster in Cytokine Receptors during Ubiquitin-independent Endosomal Sorting
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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. Accordingly, Hrs functions during ubiquitin-independent endosomal sorting of the receptors by recognizing the hydrophobic amino acid cluster. These findings suggest the existence of a group of cargo proteins that have this hydrophobic amino acid cluster as a ubiquitin-independent sorting signal.
Article
JOURNAL OF BIOLOGICAL CHEMISTRY. 286(17):15458-15472 (2011)
収録刊行物
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- JOURNAL OF BIOLOGICAL CHEMISTRY
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JOURNAL OF BIOLOGICAL CHEMISTRY 286 (17), 15458-15472, 2011-04-29
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
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詳細情報 詳細情報について
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- CRID
- 1050564288867638400
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- NII論文ID
- 120007110518
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- NII書誌ID
- AA00251083
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- HANDLE
- 10091/16885
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- ISSN
- 00219258
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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- IRDB
- CiNii Articles