The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β-protein generation
Herp is an endoplasmic reticulum (ER)-stress-inducible membrane protein, which has a ubiquitin-like domain (ULD). However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β-protein (Aβ) and that Herp...
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| Veröffentlicht in: | FEBS letters 2003-10, Vol.553 (1), p.151-156 |
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| creator | Sai, Xiaorei Kokame, Koichi Shiraishi, Hirohisa Kawamura, Yuuki Miyata, Toshiyuki Yanagisawa, Katsuhiko Komano, Hiroto |
| description | Herp is an endoplasmic reticulum (ER)-stress-inducible membrane protein, which has a ubiquitin-like domain (ULD). However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β-protein (Aβ) and that Herp interacts with presenilin (PS). Here, we addressed the role of the ULD of Herp in Aβ generation and intracellular Herp stability. We found that the ULD is not essential for the enhancement of Aβ generation by Herp expression and the interaction of Herp with PS, but is involved in the rapid degradation of Herp, most likely via the ubiquitin/proteasome pathway. Thus, the ULD of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress. |
| doi_str_mv | 10.1016/S0014-5793(03)01009-3 |
| format | Article |
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However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β-protein (Aβ) and that Herp interacts with presenilin (PS). Here, we addressed the role of the ULD of Herp in Aβ generation and intracellular Herp stability. We found that the ULD is not essential for the enhancement of Aβ generation by Herp expression and the interaction of Herp with PS, but is involved in the rapid degradation of Herp, most likely via the ubiquitin/proteasome pathway. Thus, the ULD of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(03)01009-3</identifier><identifier>PMID: 14550564</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acetylcysteine - analogs & derivatives ; Acetylcysteine - pharmacology ; AD, Alzheimer's disease ; Amino Acid Sequence ; Amyloid beta-Peptides - biosynthesis ; Amyloid beta-Peptides - metabolism ; Amyloid β-protein ; Animals ; APP, β-amyloid precursor protein ; Aβ, amyloid β-protein ; Cell Line ; Cells, Cultured ; ELISA, enzyme-linked immunosorbent assay ; Endoplasmic Reticulum - metabolism ; Endoplasmic reticulum stress ; ER, endoplasmic reticulum ; ERAD, ER-associated degradation ; Fibroblasts ; Herp ; Humans ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Peptide Fragments - biosynthesis ; Peptide Fragments - metabolism ; Presenilin ; Proteasome ; Protein Structure, Tertiary ; PS, presenilin ; Sequence Deletion - genetics ; Time Factors ; Transfection ; Ubiquitin - chemistry ; Ubiquitin - metabolism ; Ubiquitin-like domain ; ULD, ubiquitin-like domain ; ULP, ubiquitin-like protein</subject><ispartof>FEBS letters, 2003-10, Vol.553 (1), p.151-156</ispartof><rights>2003 Federation of European Biochemical Societies</rights><rights>FEBS Letters 553 (2003) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3883-3b07ebf3c5de9af3cd667a945bbf68e30c6bf11799c464cb49677481bbcfcc133</citedby><cites>FETCH-LOGICAL-c3883-3b07ebf3c5de9af3cd667a945bbf68e30c6bf11799c464cb49677481bbcfcc133</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2803%2901009-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579303010093$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14550564$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sai, Xiaorei</creatorcontrib><creatorcontrib>Kokame, Koichi</creatorcontrib><creatorcontrib>Shiraishi, Hirohisa</creatorcontrib><creatorcontrib>Kawamura, Yuuki</creatorcontrib><creatorcontrib>Miyata, Toshiyuki</creatorcontrib><creatorcontrib>Yanagisawa, Katsuhiko</creatorcontrib><creatorcontrib>Komano, Hiroto</creatorcontrib><title>The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β-protein generation</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Herp is an endoplasmic reticulum (ER)-stress-inducible membrane protein, which has a ubiquitin-like domain (ULD). However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β-protein (Aβ) and that Herp interacts with presenilin (PS). Here, we addressed the role of the ULD of Herp in Aβ generation and intracellular Herp stability. We found that the ULD is not essential for the enhancement of Aβ generation by Herp expression and the interaction of Herp with PS, but is involved in the rapid degradation of Herp, most likely via the ubiquitin/proteasome pathway. Thus, the ULD of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress.</description><subject>Acetylcysteine - analogs & derivatives</subject><subject>Acetylcysteine - pharmacology</subject><subject>AD, Alzheimer's disease</subject><subject>Amino Acid Sequence</subject><subject>Amyloid beta-Peptides - biosynthesis</subject><subject>Amyloid beta-Peptides - metabolism</subject><subject>Amyloid β-protein</subject><subject>Animals</subject><subject>APP, β-amyloid precursor protein</subject><subject>Aβ, amyloid β-protein</subject><subject>Cell Line</subject><subject>Cells, Cultured</subject><subject>ELISA, enzyme-linked immunosorbent assay</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endoplasmic reticulum stress</subject><subject>ER, endoplasmic reticulum</subject><subject>ERAD, ER-associated degradation</subject><subject>Fibroblasts</subject><subject>Herp</subject><subject>Humans</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Peptide Fragments - biosynthesis</subject><subject>Peptide Fragments - metabolism</subject><subject>Presenilin</subject><subject>Proteasome</subject><subject>Protein Structure, Tertiary</subject><subject>PS, presenilin</subject><subject>Sequence Deletion - genetics</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>Ubiquitin - chemistry</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-like domain</subject><subject>ULD, ubiquitin-like domain</subject><subject>ULP, ubiquitin-like protein</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUdtu1DAQtRCILi2fAPITAomAXV-SPCGoWrZSJR5ony1fJq0hsbd2smg_gd_hQ_gmnM0KHqlka-yZM2dmziD0gpJ3lFD5_ishlFeibtlrwt4QSkhbsUdoRZuaVYzL5jFa_YUcoWc5fyPl39D2KTqiXAgiJF-hn9d3gCfj7yc_-lD1_jtgFwftA44dXkPaYJ-xD9vYb8GVx-JzcJu006OP4S0204hDLBcs5KzTDncxYT9mDOFOBwsDhHGm08Ouj97h37-qTYojFLZbCJD2PCfoSaf7DM8P9hjdXJxfn62rqy-fL88-XlWWNU0ZzZAaTMescNDqYp2UtW65MKaTDTBipekordvWcsmt4a2sa95QY2xnLWXsGL1aeEsL9xPkUQ0-W-h7HSBOWdWilqet4AUoFqBNMecEndokP5TxFCVq3oHa70DNAitSzrwDNRd4eSgwmQHcv6yD6AWwXgA_fA-7h7Gqi_NPp_vIHCBs755rfViooCi29ZBUth6K5M4nsKNy0f-n2z8jDq1k</recordid><startdate>20031009</startdate><enddate>20031009</enddate><creator>Sai, Xiaorei</creator><creator>Kokame, Koichi</creator><creator>Shiraishi, Hirohisa</creator><creator>Kawamura, Yuuki</creator><creator>Miyata, Toshiyuki</creator><creator>Yanagisawa, Katsuhiko</creator><creator>Komano, Hiroto</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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></search><sort><creationdate>20031009</creationdate><title>The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β-protein generation</title><author>Sai, Xiaorei ; Kokame, Koichi ; Shiraishi, Hirohisa ; Kawamura, Yuuki ; Miyata, Toshiyuki ; Yanagisawa, Katsuhiko ; Komano, Hiroto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3883-3b07ebf3c5de9af3cd667a945bbf68e30c6bf11799c464cb49677481bbcfcc133</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetylcysteine - analogs & derivatives</topic><topic>Acetylcysteine - pharmacology</topic><topic>AD, Alzheimer's disease</topic><topic>Amino Acid Sequence</topic><topic>Amyloid beta-Peptides - biosynthesis</topic><topic>Amyloid beta-Peptides - metabolism</topic><topic>Amyloid β-protein</topic><topic>Animals</topic><topic>APP, β-amyloid precursor protein</topic><topic>Aβ, amyloid β-protein</topic><topic>Cell Line</topic><topic>Cells, Cultured</topic><topic>ELISA, enzyme-linked immunosorbent assay</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endoplasmic reticulum stress</topic><topic>ER, endoplasmic reticulum</topic><topic>ERAD, ER-associated degradation</topic><topic>Fibroblasts</topic><topic>Herp</topic><topic>Humans</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Peptide Fragments - biosynthesis</topic><topic>Peptide Fragments - metabolism</topic><topic>Presenilin</topic><topic>Proteasome</topic><topic>Protein Structure, Tertiary</topic><topic>PS, presenilin</topic><topic>Sequence Deletion - genetics</topic><topic>Time Factors</topic><topic>Transfection</topic><topic>Ubiquitin - chemistry</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitin-like domain</topic><topic>ULD, ubiquitin-like domain</topic><topic>ULP, ubiquitin-like protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sai, Xiaorei</creatorcontrib><creatorcontrib>Kokame, Koichi</creatorcontrib><creatorcontrib>Shiraishi, Hirohisa</creatorcontrib><creatorcontrib>Kawamura, Yuuki</creatorcontrib><creatorcontrib>Miyata, Toshiyuki</creatorcontrib><creatorcontrib>Yanagisawa, Katsuhiko</creatorcontrib><creatorcontrib>Komano, Hiroto</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sai, Xiaorei</au><au>Kokame, Koichi</au><au>Shiraishi, Hirohisa</au><au>Kawamura, Yuuki</au><au>Miyata, Toshiyuki</au><au>Yanagisawa, Katsuhiko</au><au>Komano, Hiroto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β-protein generation</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2003-10-09</date><risdate>2003</risdate><volume>553</volume><issue>1</issue><spage>151</spage><epage>156</epage><pages>151-156</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Herp is an endoplasmic reticulum (ER)-stress-inducible membrane protein, which has a ubiquitin-like domain (ULD). However, its biological function is as yet unknown. Previously, we reported that a high expression level of Herp in cells increases the generation of amyloid β-protein (Aβ) and that Herp interacts with presenilin (PS). Here, we addressed the role of the ULD of Herp in Aβ generation and intracellular Herp stability. We found that the ULD is not essential for the enhancement of Aβ generation by Herp expression and the interaction of Herp with PS, but is involved in the rapid degradation of Herp, most likely via the ubiquitin/proteasome pathway. Thus, the ULD of Herp most likely plays a role in the regulation of the intracellular level of Herp under ER stress.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>14550564</pmid><doi>10.1016/S0014-5793(03)01009-3</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2003-10, Vol.553 (1), p.151-156 |
| issn | 0014-5793 1873-3468 |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Acetylcysteine - analogs & derivatives Acetylcysteine - pharmacology AD, Alzheimer's disease Amino Acid Sequence Amyloid beta-Peptides - biosynthesis Amyloid beta-Peptides - metabolism Amyloid β-protein Animals APP, β-amyloid precursor protein Aβ, amyloid β-protein Cell Line Cells, Cultured ELISA, enzyme-linked immunosorbent assay Endoplasmic Reticulum - metabolism Endoplasmic reticulum stress ER, endoplasmic reticulum ERAD, ER-associated degradation Fibroblasts Herp Humans Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Peptide Fragments - biosynthesis Peptide Fragments - metabolism Presenilin Proteasome Protein Structure, Tertiary PS, presenilin Sequence Deletion - genetics Time Factors Transfection Ubiquitin - chemistry Ubiquitin - metabolism Ubiquitin-like domain ULD, ubiquitin-like domain ULP, ubiquitin-like protein |
| title | The ubiquitin-like domain of Herp is involved in Herp degradation, but not necessary for its enhancement of amyloid β-protein generation |
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