AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination
Activating molecule in Beclin-1-regulated autophagy (AMBRA1), a negative regulator of tumorigenesis, is a substrate receptor of the ubiquitin conjugation system. ALDH1B1, an aldehyde dehydrogenase, is a cancer stem cell (CSC) marker that is required for carcinogenesis via upregulation of the β-caten...
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| description | Activating molecule in Beclin-1-regulated autophagy (AMBRA1), a negative regulator of tumorigenesis, is a substrate receptor of the ubiquitin conjugation system. ALDH1B1, an aldehyde dehydrogenase, is a cancer stem cell (CSC) marker that is required for carcinogenesis via upregulation of the β-catenin pathway. Although accumulating evidence suggests a role for ubiquitination in the regulation of CSC markers, the ubiquitination-mediated regulation of ALDH1B1 has not been unraveled. While proteome analysis has suggested that AMBRA1 and ALDH1B1 can interact, their interaction has not been validated. Here, we show that AMBRA1 is a negative regulator of ALDH1B1. The expression of ALDH1B1-regulated genes, including
,
(β-catenin), and CSC-related β-catenin target genes, is inversely regulated by AMBRA1, suggesting a negative regulatory role of AMBRA1 in the expression of ALDH1B1-regulated genes. We found that the K27- and K33-linked ubiquitination of ALDH1B1 is mediated via the cooperation of AMBRA1 with other E3 ligases, such as TRAF6. Importantly, ubiquitination site mapping revealed that K506, K511, and K515 are important for the K27-linked ubiquitination of ALDH1B1, while K33-linked ubiquitination occurs at K506. A ubiquitination-defective mutant of ALDH1B1 increased the self-association ability of ALDH1B1, suggesting a negative correlation between the ubiquitination and self-association of ALDH1B1. Together, our findings indicate that ALDH1B1 is negatively regulated by AMBRA1-mediated noncanonical ubiquitination. |
| doi_str_mv | 10.3390/ijms222112079 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8584921</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2596040013</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-4ce66848644e78443862d6dd5ca578d16d7675afd164103ad7e9bcb43a00165f3</originalsourceid><addsrcrecordid>eNpVkUtLxDAUhYMovpduJeDWal5N2o0wU18Do4KPdUjb2zFjp3GSVJh_bwcf6OoeuB_nHu5B6IiSM85zcm7ni8AYo5QRlW-gXSoYSwiRavOP3kF7IcwJYZyl-Tba4ULJPCVqFy1Hd-PHEcX3MDPRfkC7wo8w61sTIeD4Cvi676poXYddg0fTy1s6pqfY4MJ0FXj8FGGBC2hbfGf8G_hTXK5w4broXdvaboYnMeCX0i57G21n1kYHaKsxbYDD77mPXq6vnovbZPpwMylG06QSNI2JqEDKTGRSCFCZEDyTrJZ1nVYmVVlNZa2kSk0zKEEJN7WCvKxKwQ0hVKYN30cXX77vfbmAuoIhlGn1u7cL41faGav_bzr7qmfuQ2dpJnJGB4OTbwPvlj2EqOeu992QWQ9flEQMh_hAJV9U5V0IHprfC5TodUP6X0MDf_w31i_9Uwn_BJRFi40</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2596040013</pqid></control><display><type>article</type><title>AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination</title><source>MDPI - Multidisciplinary Digital Publishing Institute</source><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Baek, Seung-Heon ; Jang, Yeun-Kyu</creator><creatorcontrib>Baek, Seung-Heon ; Jang, Yeun-Kyu</creatorcontrib><description>Activating molecule in Beclin-1-regulated autophagy (AMBRA1), a negative regulator of tumorigenesis, is a substrate receptor of the ubiquitin conjugation system. ALDH1B1, an aldehyde dehydrogenase, is a cancer stem cell (CSC) marker that is required for carcinogenesis via upregulation of the β-catenin pathway. Although accumulating evidence suggests a role for ubiquitination in the regulation of CSC markers, the ubiquitination-mediated regulation of ALDH1B1 has not been unraveled. While proteome analysis has suggested that AMBRA1 and ALDH1B1 can interact, their interaction has not been validated. Here, we show that AMBRA1 is a negative regulator of ALDH1B1. The expression of ALDH1B1-regulated genes, including
,
(β-catenin), and CSC-related β-catenin target genes, is inversely regulated by AMBRA1, suggesting a negative regulatory role of AMBRA1 in the expression of ALDH1B1-regulated genes. We found that the K27- and K33-linked ubiquitination of ALDH1B1 is mediated via the cooperation of AMBRA1 with other E3 ligases, such as TRAF6. Importantly, ubiquitination site mapping revealed that K506, K511, and K515 are important for the K27-linked ubiquitination of ALDH1B1, while K33-linked ubiquitination occurs at K506. A ubiquitination-defective mutant of ALDH1B1 increased the self-association ability of ALDH1B1, suggesting a negative correlation between the ubiquitination and self-association of ALDH1B1. Together, our findings indicate that ALDH1B1 is negatively regulated by AMBRA1-mediated noncanonical ubiquitination.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms222112079</identifier><identifier>PMID: 34769507</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Aldehyde dehydrogenase ; Aldehyde Dehydrogenase 1 Family - antagonists & inhibitors ; Aldehyde Dehydrogenase 1 Family - metabolism ; Aldehyde Dehydrogenase, Mitochondrial - antagonists & inhibitors ; Aldehyde Dehydrogenase, Mitochondrial - metabolism ; Aldehydes ; Autophagy ; beta Catenin - metabolism ; Carcinogenesis ; Carcinogens ; Cell Line ; Cell Line, Tumor ; Colorectal cancer ; Conjugation ; Defective mutant ; Enzymes ; Gene expression ; Genes ; Humans ; Neoplastic Stem Cells - metabolism ; Neoplastic Stem Cells - pathology ; Phagocytosis ; Proteins ; Proteomes ; PTEN protein ; Self-association ; Stem cells ; TNF Receptor-Associated Factor 6 - metabolism ; TRAF6 protein ; Tumorigenesis ; Ubiquitin ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination ; Wnt Signaling Pathway ; β-Catenin</subject><ispartof>International journal of molecular sciences, 2021-11, Vol.22 (21), p.12079</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-4ce66848644e78443862d6dd5ca578d16d7675afd164103ad7e9bcb43a00165f3</citedby><cites>FETCH-LOGICAL-c415t-4ce66848644e78443862d6dd5ca578d16d7675afd164103ad7e9bcb43a00165f3</cites><orcidid>0000-0002-1342-4190 ; 0000-0003-1793-1576</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8584921/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8584921/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34769507$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baek, Seung-Heon</creatorcontrib><creatorcontrib>Jang, Yeun-Kyu</creatorcontrib><title>AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination</title><title>International journal of molecular sciences</title><addtitle>Int J Mol Sci</addtitle><description>Activating molecule in Beclin-1-regulated autophagy (AMBRA1), a negative regulator of tumorigenesis, is a substrate receptor of the ubiquitin conjugation system. ALDH1B1, an aldehyde dehydrogenase, is a cancer stem cell (CSC) marker that is required for carcinogenesis via upregulation of the β-catenin pathway. Although accumulating evidence suggests a role for ubiquitination in the regulation of CSC markers, the ubiquitination-mediated regulation of ALDH1B1 has not been unraveled. While proteome analysis has suggested that AMBRA1 and ALDH1B1 can interact, their interaction has not been validated. Here, we show that AMBRA1 is a negative regulator of ALDH1B1. The expression of ALDH1B1-regulated genes, including
,
(β-catenin), and CSC-related β-catenin target genes, is inversely regulated by AMBRA1, suggesting a negative regulatory role of AMBRA1 in the expression of ALDH1B1-regulated genes. We found that the K27- and K33-linked ubiquitination of ALDH1B1 is mediated via the cooperation of AMBRA1 with other E3 ligases, such as TRAF6. Importantly, ubiquitination site mapping revealed that K506, K511, and K515 are important for the K27-linked ubiquitination of ALDH1B1, while K33-linked ubiquitination occurs at K506. A ubiquitination-defective mutant of ALDH1B1 increased the self-association ability of ALDH1B1, suggesting a negative correlation between the ubiquitination and self-association of ALDH1B1. Together, our findings indicate that ALDH1B1 is negatively regulated by AMBRA1-mediated noncanonical ubiquitination.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Aldehyde dehydrogenase</subject><subject>Aldehyde Dehydrogenase 1 Family - antagonists & inhibitors</subject><subject>Aldehyde Dehydrogenase 1 Family - metabolism</subject><subject>Aldehyde Dehydrogenase, Mitochondrial - antagonists & inhibitors</subject><subject>Aldehyde Dehydrogenase, Mitochondrial - metabolism</subject><subject>Aldehydes</subject><subject>Autophagy</subject><subject>beta Catenin - metabolism</subject><subject>Carcinogenesis</subject><subject>Carcinogens</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Colorectal cancer</subject><subject>Conjugation</subject><subject>Defective mutant</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Genes</subject><subject>Humans</subject><subject>Neoplastic Stem Cells - metabolism</subject><subject>Neoplastic Stem Cells - pathology</subject><subject>Phagocytosis</subject><subject>Proteins</subject><subject>Proteomes</subject><subject>PTEN protein</subject><subject>Self-association</subject><subject>Stem cells</subject><subject>TNF Receptor-Associated Factor 6 - metabolism</subject><subject>TRAF6 protein</subject><subject>Tumorigenesis</subject><subject>Ubiquitin</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitination</subject><subject>Wnt Signaling Pathway</subject><subject>β-Catenin</subject><issn>1422-0067</issn><issn>1661-6596</issn><issn>1422-0067</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpVkUtLxDAUhYMovpduJeDWal5N2o0wU18Do4KPdUjb2zFjp3GSVJh_bwcf6OoeuB_nHu5B6IiSM85zcm7ni8AYo5QRlW-gXSoYSwiRavOP3kF7IcwJYZyl-Tba4ULJPCVqFy1Hd-PHEcX3MDPRfkC7wo8w61sTIeD4Cvi676poXYddg0fTy1s6pqfY4MJ0FXj8FGGBC2hbfGf8G_hTXK5w4broXdvaboYnMeCX0i57G21n1kYHaKsxbYDD77mPXq6vnovbZPpwMylG06QSNI2JqEDKTGRSCFCZEDyTrJZ1nVYmVVlNZa2kSk0zKEEJN7WCvKxKwQ0hVKYN30cXX77vfbmAuoIhlGn1u7cL41faGav_bzr7qmfuQ2dpJnJGB4OTbwPvlj2EqOeu992QWQ9flEQMh_hAJV9U5V0IHprfC5TodUP6X0MDf_w31i_9Uwn_BJRFi40</recordid><startdate>20211108</startdate><enddate>20211108</enddate><creator>Baek, Seung-Heon</creator><creator>Jang, Yeun-Kyu</creator><general>MDPI AG</general><general>MDPI</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1342-4190</orcidid><orcidid>https://orcid.org/0000-0003-1793-1576</orcidid></search><sort><creationdate>20211108</creationdate><title>AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination</title><author>Baek, Seung-Heon ; Jang, Yeun-Kyu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-4ce66848644e78443862d6dd5ca578d16d7675afd164103ad7e9bcb43a00165f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Aldehyde dehydrogenase</topic><topic>Aldehyde Dehydrogenase 1 Family - antagonists & inhibitors</topic><topic>Aldehyde Dehydrogenase 1 Family - metabolism</topic><topic>Aldehyde Dehydrogenase, Mitochondrial - antagonists & inhibitors</topic><topic>Aldehyde Dehydrogenase, Mitochondrial - metabolism</topic><topic>Aldehydes</topic><topic>Autophagy</topic><topic>beta Catenin - metabolism</topic><topic>Carcinogenesis</topic><topic>Carcinogens</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Colorectal cancer</topic><topic>Conjugation</topic><topic>Defective mutant</topic><topic>Enzymes</topic><topic>Gene expression</topic><topic>Genes</topic><topic>Humans</topic><topic>Neoplastic Stem Cells - metabolism</topic><topic>Neoplastic Stem Cells - pathology</topic><topic>Phagocytosis</topic><topic>Proteins</topic><topic>Proteomes</topic><topic>PTEN protein</topic><topic>Self-association</topic><topic>Stem cells</topic><topic>TNF Receptor-Associated Factor 6 - metabolism</topic><topic>TRAF6 protein</topic><topic>Tumorigenesis</topic><topic>Ubiquitin</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>Ubiquitination</topic><topic>Wnt Signaling Pathway</topic><topic>β-Catenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baek, Seung-Heon</creatorcontrib><creatorcontrib>Jang, Yeun-Kyu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baek, Seung-Heon</au><au>Jang, Yeun-Kyu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-11-08</date><risdate>2021</risdate><volume>22</volume><issue>21</issue><spage>12079</spage><pages>12079-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Activating molecule in Beclin-1-regulated autophagy (AMBRA1), a negative regulator of tumorigenesis, is a substrate receptor of the ubiquitin conjugation system. ALDH1B1, an aldehyde dehydrogenase, is a cancer stem cell (CSC) marker that is required for carcinogenesis via upregulation of the β-catenin pathway. Although accumulating evidence suggests a role for ubiquitination in the regulation of CSC markers, the ubiquitination-mediated regulation of ALDH1B1 has not been unraveled. While proteome analysis has suggested that AMBRA1 and ALDH1B1 can interact, their interaction has not been validated. Here, we show that AMBRA1 is a negative regulator of ALDH1B1. The expression of ALDH1B1-regulated genes, including
,
(β-catenin), and CSC-related β-catenin target genes, is inversely regulated by AMBRA1, suggesting a negative regulatory role of AMBRA1 in the expression of ALDH1B1-regulated genes. We found that the K27- and K33-linked ubiquitination of ALDH1B1 is mediated via the cooperation of AMBRA1 with other E3 ligases, such as TRAF6. Importantly, ubiquitination site mapping revealed that K506, K511, and K515 are important for the K27-linked ubiquitination of ALDH1B1, while K33-linked ubiquitination occurs at K506. A ubiquitination-defective mutant of ALDH1B1 increased the self-association ability of ALDH1B1, suggesting a negative correlation between the ubiquitination and self-association of ALDH1B1. Together, our findings indicate that ALDH1B1 is negatively regulated by AMBRA1-mediated noncanonical ubiquitination.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>34769507</pmid><doi>10.3390/ijms222112079</doi><orcidid>https://orcid.org/0000-0002-1342-4190</orcidid><orcidid>https://orcid.org/0000-0003-1793-1576</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - metabolism Aldehyde dehydrogenase Aldehyde Dehydrogenase 1 Family - antagonists & inhibitors Aldehyde Dehydrogenase 1 Family - metabolism Aldehyde Dehydrogenase, Mitochondrial - antagonists & inhibitors Aldehyde Dehydrogenase, Mitochondrial - metabolism Aldehydes Autophagy beta Catenin - metabolism Carcinogenesis Carcinogens Cell Line Cell Line, Tumor Colorectal cancer Conjugation Defective mutant Enzymes Gene expression Genes Humans Neoplastic Stem Cells - metabolism Neoplastic Stem Cells - pathology Phagocytosis Proteins Proteomes PTEN protein Self-association Stem cells TNF Receptor-Associated Factor 6 - metabolism TRAF6 protein Tumorigenesis Ubiquitin Ubiquitin-Protein Ligases - metabolism Ubiquitination Wnt Signaling Pathway β-Catenin |
| title | AMBRA1 Negatively Regulates the Function of ALDH1B1, a Cancer Stem Cell Marker, by Controlling Its Ubiquitination |
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