A novel ER α-mannosidase-like protein accelerates ER-associated degradation
The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded proteins are retrotranslocated from the ER and degraded by cytoplasmic proteasomes, a mechanism known as ER‐associated d...
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| Veröffentlicht in: | EMBO reports 2001-05, Vol.2 (5), p.415-422 |
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| creator | Hosokawa, Nobuko Wada, Ikuo Hasegawa, Kiyotaka Yorihuzi, Tetuya Tremblay, Linda O Herscovics, Annette Nagata, Kazuhiro |
| description | The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded proteins are retrotranslocated from the ER and degraded by cytoplasmic proteasomes, a mechanism known as ER‐associated degradation (ERAD). We report the cDNA cloning of
Edem
, a mouse gene encoding a putative type II ER transmembrane protein. Expression of
Edem
mRNA was induced by various types of ER stress. Although the luminal region of
E
R
d
egradation
e
nhancing α‐
m
annosidase‐like protein (EDEM) is similar to class I α1,2‐mannosidases involved in
N
‐glycan processing, EDEM did not have enzymatic activity. Overexpression of EDEM in human embryonic kidney 293 cells accelerated the degradation of misfolded α1‐antitrypsin, and EDEM bound to this misfolded glycoprotein. The results suggest that EDEM is directly involved in ERAD, and targets misfolded glycoproteins for degradation in an
N
‐glycan dependent manner. |
| doi_str_mv | 10.1093/embo-reports/kve084 |
| format | Article |
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Edem
, a mouse gene encoding a putative type II ER transmembrane protein. Expression of
Edem
mRNA was induced by various types of ER stress. Although the luminal region of
E
R
d
egradation
e
nhancing α‐
m
annosidase‐like protein (EDEM) is similar to class I α1,2‐mannosidases involved in
N
‐glycan processing, EDEM did not have enzymatic activity. Overexpression of EDEM in human embryonic kidney 293 cells accelerated the degradation of misfolded α1‐antitrypsin, and EDEM bound to this misfolded glycoprotein. The results suggest that EDEM is directly involved in ERAD, and targets misfolded glycoproteins for degradation in an
N
‐glycan dependent manner.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.1093/embo-reports/kve084</identifier><identifier>PMID: 11375934</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Alkaloids - pharmacology ; alpha 1-Antitrypsin - chemistry ; alpha 1-Antitrypsin - metabolism ; alpha-Mannosidase ; Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Endoplasmic Reticulum - chemistry ; Endoplasmic Reticulum - metabolism ; Enzyme Inhibitors - pharmacology ; Gene Expression Regulation - genetics ; Glycoproteins - metabolism ; Humans ; Mannosidases - antagonists & inhibitors ; Mannosidases - genetics ; Mannosidases - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Molecular Sequence Data ; Protein Folding ; Rabbits ; RNA - genetics ; RNA - metabolism ; Scientific Report ; Scientific Reports ; Sequence Alignment ; Serine Proteinase Inhibitors - metabolism ; Transfection</subject><ispartof>EMBO reports, 2001-05, Vol.2 (5), p.415-422</ispartof><rights>European Molecular Biology Organization 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5331-afc43d08be6ae29f32516936d35100b75199a1f9128a4b42f817ffad26e824e53</citedby><cites>FETCH-LOGICAL-c5331-afc43d08be6ae29f32516936d35100b75199a1f9128a4b42f817ffad26e824e53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083879/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1083879/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11375934$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hosokawa, Nobuko</creatorcontrib><creatorcontrib>Wada, Ikuo</creatorcontrib><creatorcontrib>Hasegawa, Kiyotaka</creatorcontrib><creatorcontrib>Yorihuzi, Tetuya</creatorcontrib><creatorcontrib>Tremblay, Linda O</creatorcontrib><creatorcontrib>Herscovics, Annette</creatorcontrib><creatorcontrib>Nagata, Kazuhiro</creatorcontrib><title>A novel ER α-mannosidase-like protein accelerates ER-associated degradation</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded proteins are retrotranslocated from the ER and degraded by cytoplasmic proteasomes, a mechanism known as ER‐associated degradation (ERAD). We report the cDNA cloning of
Edem
, a mouse gene encoding a putative type II ER transmembrane protein. Expression of
Edem
mRNA was induced by various types of ER stress. Although the luminal region of
E
R
d
egradation
e
nhancing α‐
m
annosidase‐like protein (EDEM) is similar to class I α1,2‐mannosidases involved in
N
‐glycan processing, EDEM did not have enzymatic activity. Overexpression of EDEM in human embryonic kidney 293 cells accelerated the degradation of misfolded α1‐antitrypsin, and EDEM bound to this misfolded glycoprotein. The results suggest that EDEM is directly involved in ERAD, and targets misfolded glycoproteins for degradation in an
N
‐glycan dependent manner.</description><subject>Alkaloids - pharmacology</subject><subject>alpha 1-Antitrypsin - chemistry</subject><subject>alpha 1-Antitrypsin - metabolism</subject><subject>alpha-Mannosidase</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cloning, Molecular</subject><subject>Endoplasmic Reticulum - chemistry</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gene Expression Regulation - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>Humans</subject><subject>Mannosidases - antagonists & inhibitors</subject><subject>Mannosidases - genetics</subject><subject>Mannosidases - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Protein Folding</subject><subject>Rabbits</subject><subject>RNA - genetics</subject><subject>RNA - metabolism</subject><subject>Scientific Report</subject><subject>Scientific Reports</subject><subject>Sequence Alignment</subject><subject>Serine Proteinase Inhibitors - metabolism</subject><subject>Transfection</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUhS1ERUvhCZBQVuxM_ZfY3iCV0TBUmoJUgWBnOcnN4E5iD3ZmoI_Fi_SZ6ipRgRWsbOue79zrexB6QclrSjQ_g6EOOMIuxDGdbQ9AlHiETqioNOZUqsfznTH69Rg9TemaEFJqqZ6gY0q5LDUXJ2h9XvhwgL5YXhW3v_BgvQ_JtTYB7t0Wil0MIzhf2KaBHqIdIWUptimFxuVXW7Swiba1owv-GTrqbJ_g-Xyeos_vlp8W7_H64-picb7GTck5xbZrBG-JqqGywHTHWUkrzauWl5SQWpZUa0s7TZmyohasU1R2nW1ZBYoJKPkpejP57vb1AG0Dfoy2N7voBhtvTLDO_F3x7pvZhIOhRHEldTZ4NRvE8H0PaTSDS_mDvfUQ9slIoipNJctCPgmbGFKK0D00ocTcp2DuUzBzCmZKIVMv_5zvNzOvPQvUJPjherj5H0-zvHx7JTjNqJjQlCm_gWiuwz76vO5_jIQnzKURfj50tHFrKpmnMl8-rMxlJRjhamUW_A5cRb7z</recordid><startdate>200105</startdate><enddate>200105</enddate><creator>Hosokawa, Nobuko</creator><creator>Wada, Ikuo</creator><creator>Hasegawa, Kiyotaka</creator><creator>Yorihuzi, Tetuya</creator><creator>Tremblay, Linda O</creator><creator>Herscovics, Annette</creator><creator>Nagata, Kazuhiro</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Oxford University Press</general><scope>BSCLL</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><scope>5PM</scope></search><sort><creationdate>200105</creationdate><title>A novel ER α-mannosidase-like protein accelerates ER-associated degradation</title><author>Hosokawa, Nobuko ; Wada, Ikuo ; Hasegawa, Kiyotaka ; Yorihuzi, Tetuya ; Tremblay, Linda O ; Herscovics, Annette ; Nagata, Kazuhiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5331-afc43d08be6ae29f32516936d35100b75199a1f9128a4b42f817ffad26e824e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Alkaloids - pharmacology</topic><topic>alpha 1-Antitrypsin - chemistry</topic><topic>alpha 1-Antitrypsin - metabolism</topic><topic>alpha-Mannosidase</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Cloning, Molecular</topic><topic>Endoplasmic Reticulum - chemistry</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Gene Expression Regulation - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>Humans</topic><topic>Mannosidases - antagonists & inhibitors</topic><topic>Mannosidases - genetics</topic><topic>Mannosidases - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Protein Folding</topic><topic>Rabbits</topic><topic>RNA - genetics</topic><topic>RNA - metabolism</topic><topic>Scientific Report</topic><topic>Scientific Reports</topic><topic>Sequence Alignment</topic><topic>Serine Proteinase Inhibitors - metabolism</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hosokawa, Nobuko</creatorcontrib><creatorcontrib>Wada, Ikuo</creatorcontrib><creatorcontrib>Hasegawa, Kiyotaka</creatorcontrib><creatorcontrib>Yorihuzi, Tetuya</creatorcontrib><creatorcontrib>Tremblay, Linda O</creatorcontrib><creatorcontrib>Herscovics, Annette</creatorcontrib><creatorcontrib>Nagata, Kazuhiro</creatorcontrib><collection>Istex</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hosokawa, Nobuko</au><au>Wada, Ikuo</au><au>Hasegawa, Kiyotaka</au><au>Yorihuzi, Tetuya</au><au>Tremblay, Linda O</au><au>Herscovics, Annette</au><au>Nagata, Kazuhiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel ER α-mannosidase-like protein accelerates ER-associated degradation</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2001-05</date><risdate>2001</risdate><volume>2</volume><issue>5</issue><spage>415</spage><epage>422</epage><pages>415-422</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><abstract>The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded proteins are retrotranslocated from the ER and degraded by cytoplasmic proteasomes, a mechanism known as ER‐associated degradation (ERAD). We report the cDNA cloning of
Edem
, a mouse gene encoding a putative type II ER transmembrane protein. Expression of
Edem
mRNA was induced by various types of ER stress. Although the luminal region of
E
R
d
egradation
e
nhancing α‐
m
annosidase‐like protein (EDEM) is similar to class I α1,2‐mannosidases involved in
N
‐glycan processing, EDEM did not have enzymatic activity. Overexpression of EDEM in human embryonic kidney 293 cells accelerated the degradation of misfolded α1‐antitrypsin, and EDEM bound to this misfolded glycoprotein. The results suggest that EDEM is directly involved in ERAD, and targets misfolded glycoproteins for degradation in an
N
‐glycan dependent manner.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11375934</pmid><doi>10.1093/embo-reports/kve084</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1469-221X |
| ispartof | EMBO reports, 2001-05, Vol.2 (5), p.415-422 |
| issn | 1469-221X 1469-3178 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083879 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Alkaloids - pharmacology alpha 1-Antitrypsin - chemistry alpha 1-Antitrypsin - metabolism alpha-Mannosidase Amino Acid Sequence Animals Cell Line Cloning, Molecular Endoplasmic Reticulum - chemistry Endoplasmic Reticulum - metabolism Enzyme Inhibitors - pharmacology Gene Expression Regulation - genetics Glycoproteins - metabolism Humans Mannosidases - antagonists & inhibitors Mannosidases - genetics Mannosidases - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Molecular Sequence Data Protein Folding Rabbits RNA - genetics RNA - metabolism Scientific Report Scientific Reports Sequence Alignment Serine Proteinase Inhibitors - metabolism Transfection |
| title | A novel ER α-mannosidase-like protein accelerates ER-associated degradation |
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