STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif
Conjugation with ubiquitin acts as a sorting signal for proteins in the endocytic and biosynthetic pathways at the endosome. Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown...
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| Veröffentlicht in: | Molecular biology of the cell 2003-09, Vol.14 (9), p.3675-3689 |
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| container_issue | 9 |
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| container_title | Molecular biology of the cell |
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| creator | Mizuno, Emi Kawahata, Kensuke Kato, Masaki Kitamura, Naomi Komada, Masayuki |
| description | Conjugation with ubiquitin acts as a sorting signal for proteins in the endocytic and biosynthetic pathways at the endosome. Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown. Herein, we show that STAM proteins bind ubiquitin and ubiquitinated proteins and that the tandemly located VHS (Vps27/Hrs/STAM) domain and ubiquitin-interacting motif serve as the binding site(s). STAM proteins colocalize with Hrs on the early endosome. Overexpression of STAM proteins, but not their mutants lacking the ubiquitin-binding activity, causes the accumulation of ubiquitinated proteins and ligand-activated epidermal growth factor receptor on the early endosome. These results suggest that through interaction with ubiquitinated cargo proteins on the early endosome via the VHS domain and ubiquitin-interacting motif, STAM proteins participate in the sorting of cargo proteins for trafficking to the lysosome. |
| doi_str_mv | 10.1091/mbc.E02-12-0823 |
| format | Article |
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Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown. Herein, we show that STAM proteins bind ubiquitin and ubiquitinated proteins and that the tandemly located VHS (Vps27/Hrs/STAM) domain and ubiquitin-interacting motif serve as the binding site(s). STAM proteins colocalize with Hrs on the early endosome. Overexpression of STAM proteins, but not their mutants lacking the ubiquitin-binding activity, causes the accumulation of ubiquitinated proteins and ligand-activated epidermal growth factor receptor on the early endosome. 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Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown. Herein, we show that STAM proteins bind ubiquitin and ubiquitinated proteins and that the tandemly located VHS (Vps27/Hrs/STAM) domain and ubiquitin-interacting motif serve as the binding site(s). STAM proteins colocalize with Hrs on the early endosome. Overexpression of STAM proteins, but not their mutants lacking the ubiquitin-binding activity, causes the accumulation of ubiquitinated proteins and ligand-activated epidermal growth factor receptor on the early endosome. These results suggest that through interaction with ubiquitinated cargo proteins on the early endosome via the VHS domain and ubiquitin-interacting motif, STAM proteins participate in the sorting of cargo proteins for trafficking to the lysosome.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>Endocytosis - physiology</subject><subject>Endosomal Sorting Complexes Required for Transport</subject><subject>Endosomes - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Phosphoproteins - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Ubiquitin - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUblOxTAQtBCIu6ZDrugCPmOnoECISwJRcLSW42zAKLEftoPE3xPgiaPa0c7M7moHoT1KDilp6NHYusMzwirKKqIZX0GbtOFNJaSuV2dMZFNRycQG2sr5hRAqRK3W0QZljWJS1pso3d2f3OBFigV8yLj1ocNT618nX3ywBbpfLgZcngGDTcM7htDFHEfAb95-tR8v73AXR-sDtn9nVD4USNbN8AmPsfh-B631dsiwu6zb6OH87P70srq-vbg6PbmunFSyVJI4zoAT6azUPe17oRUn0LZK94Jr2lPFoCbCdVZQK5RWpNa207JrnWyp49vo-HvuYmpH6ByEkuxgFsmPNr2baL35zwT_bJ7im6FNLWUz-w-W_hRfJ8jFjD47GAYbIE7ZKF4LMn97Fh59C12KOSfof3ZQYj5jMnNMBggzlJnPmGbH_t_TfvXLXPgHtOORwg</recordid><startdate>20030901</startdate><enddate>20030901</enddate><creator>Mizuno, Emi</creator><creator>Kawahata, Kensuke</creator><creator>Kato, Masaki</creator><creator>Kitamura, Naomi</creator><creator>Komada, Masayuki</creator><general>The American Society for Cell Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20030901</creationdate><title>STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif</title><author>Mizuno, Emi ; Kawahata, Kensuke ; Kato, Masaki ; Kitamura, Naomi ; Komada, Masayuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c575t-50c32e305ca58f1ff48730ebb78f4381f172e604cda41a4787068ad85dbc5b1c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>Endocytosis - physiology</topic><topic>Endosomal Sorting Complexes Required for Transport</topic><topic>Endosomes - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Phosphoproteins - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>Ubiquitin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mizuno, Emi</creatorcontrib><creatorcontrib>Kawahata, Kensuke</creatorcontrib><creatorcontrib>Kato, Masaki</creatorcontrib><creatorcontrib>Kitamura, Naomi</creatorcontrib><creatorcontrib>Komada, Masayuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mizuno, Emi</au><au>Kawahata, Kensuke</au><au>Kato, Masaki</au><au>Kitamura, Naomi</au><au>Komada, Masayuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2003-09-01</date><risdate>2003</risdate><volume>14</volume><issue>9</issue><spage>3675</spage><epage>3689</epage><pages>3675-3689</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Conjugation with ubiquitin acts as a sorting signal for proteins in the endocytic and biosynthetic pathways at the endosome. Signal-transducing adaptor molecule (STAM) proteins, STAM1 and STAM2, are associated with hepatocyte growth factor-regulated substrate (Hrs) but their function remains unknown. Herein, we show that STAM proteins bind ubiquitin and ubiquitinated proteins and that the tandemly located VHS (Vps27/Hrs/STAM) domain and ubiquitin-interacting motif serve as the binding site(s). STAM proteins colocalize with Hrs on the early endosome. Overexpression of STAM proteins, but not their mutants lacking the ubiquitin-binding activity, causes the accumulation of ubiquitinated proteins and ligand-activated epidermal growth factor receptor on the early endosome. 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| ispartof | Molecular biology of the cell, 2003-09, Vol.14 (9), p.3675-3689 |
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| subjects | Adaptor Proteins, Signal Transducing Animals Cercopithecus aethiops COS Cells Endocytosis - physiology Endosomal Sorting Complexes Required for Transport Endosomes - metabolism HeLa Cells Humans Phosphoproteins - metabolism Protein Structure, Tertiary Protein Transport Receptor, Epidermal Growth Factor - metabolism Ubiquitin - metabolism |
| title | STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif |
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