Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity
Prominin‐1 (Prom1) is a major cell surface marker of cancer stem cells, but its physiological functions in the liver have not been elucidated. We analyzed the levels of mRNA transcripts in serum‐starved primary WT ( Prom1 +/+ ) and KO ( Prom1 −/− ) mouse hepatocytes using RNA sequencing (RNA‐seq) da...
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| description | Prominin‐1 (Prom1) is a major cell surface marker of cancer stem cells, but its physiological functions in the liver have not been elucidated. We analyzed the levels of mRNA transcripts in serum‐starved primary WT (
Prom1
+/+
) and KO (
Prom1
−/−
) mouse hepatocytes using RNA sequencing (RNA‐seq) data, and found that CREB target genes were downregulated. This initial observation led us to determine that Prom1 deficiency inhibited cAMP response element‐binding protein (CREB) activation and gluconeogenesis, but not cyclic AMP (cAMP) accumulation, in glucagon‐, epinephrine‐, or forskolin‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐induced hyperglycemia. Because Prom1 interacted with radixin, Prom1 deficiency prevented radixin from localizing to the plasma membrane. Moreover, systemic adenoviral knockdown of radixin inhibited CREB activation and gluconeogenesis in glucagon‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐elicited hyperglycemia. Based on these results, we conclude that Prom1 regulates hepatic PKA signaling via radixin functioning as an A kinase‐anchored protein (AKAP).
Synopsis
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.
The transmembrane protein Prominin‐1 is expressed in hepatocytes as well as cholangiocytes in the liver.
Prominin‐1 functions as an anchor for radixin, which brings PKA holoenzyme to membrane microdomains, where local cAMP concentration is increased by glucagon‐induced activation of adenylyl cyclase.
Prom1 knockout and knockdown result in inhibition of glucagon‐elicited CREB phosphorylation and gluconeogenesis in hepatocytes and livers.
Graphical Abstract
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein. |
| doi_str_mv | 10.15252/embr.201949416 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_C6C</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7645247</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2457846390</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5796-53a8f45b578d5799caee028e37432bfdcc97796f4420093e8f3b8e8ae85343ee3</originalsourceid><addsrcrecordid>eNqFkU9PFTEUxRuiAUTW7swkbtg86N-Z1oUJEAQjRkIguGs6fXeGkpn20c4gb-dH4DPySay-5xNNjIumze3vnpyTg9ArgneJoILuQV_HXYqJ4oqTcg1tEl6qCSOVfLZ8U0q-bKAXKd1gjIWq5DraYAwzLDHdRFdnMfTOO__47YHkc26m7t75wty7VNjghxi6VFzDzAzOFm035hmEFjykDNTzIkI7dvnTt8XZx_3C2MHduWH-Ej1vTJdge3lvocv3RxeHJ5PTz8cfDvdPJ1ZUqpwIZmTDRS0qOc0DZQ0AphJYxRmtm6m1qspcwznFWDGQDaslSANSMM4A2BZ6t9CdjXUPUwvZsen0LLrexLkOxuk_f7y71m2401XJBeVVFthZCsRwO0IadO-Sha4zOeeYNOVc0ZIRLjL65i_0JozR53iZygl4yRTO1N6CsjGkFKFZmSFY_yxN_yhNr0rLG6-fZljxv1rKwNsF8NV1MP-fnj76dHD-VB0vllPe8y3E367_Zeg7hg23AA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2457846390</pqid></control><display><type>article</type><title>Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity</title><source>Springer Nature OA Free Journals</source><creator>Lee, Hyun ; Yu, Dong‐Min ; Park, Jun Sub ; Lee, Hwayeon ; Kim, Jun‐Seok ; Kim, Hong Lim ; Koo, Seung‐Hoi ; Lee, Jae‐Seon ; Lee, Sungsoo ; Ko, Young‐Gyu</creator><creatorcontrib>Lee, Hyun ; Yu, Dong‐Min ; Park, Jun Sub ; Lee, Hwayeon ; Kim, Jun‐Seok ; Kim, Hong Lim ; Koo, Seung‐Hoi ; Lee, Jae‐Seon ; Lee, Sungsoo ; Ko, Young‐Gyu</creatorcontrib><description>Prominin‐1 (Prom1) is a major cell surface marker of cancer stem cells, but its physiological functions in the liver have not been elucidated. We analyzed the levels of mRNA transcripts in serum‐starved primary WT (
Prom1
+/+
) and KO (
Prom1
−/−
) mouse hepatocytes using RNA sequencing (RNA‐seq) data, and found that CREB target genes were downregulated. This initial observation led us to determine that Prom1 deficiency inhibited cAMP response element‐binding protein (CREB) activation and gluconeogenesis, but not cyclic AMP (cAMP) accumulation, in glucagon‐, epinephrine‐, or forskolin‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐induced hyperglycemia. Because Prom1 interacted with radixin, Prom1 deficiency prevented radixin from localizing to the plasma membrane. Moreover, systemic adenoviral knockdown of radixin inhibited CREB activation and gluconeogenesis in glucagon‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐elicited hyperglycemia. Based on these results, we conclude that Prom1 regulates hepatic PKA signaling via radixin functioning as an A kinase‐anchored protein (AKAP).
Synopsis
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.
The transmembrane protein Prominin‐1 is expressed in hepatocytes as well as cholangiocytes in the liver.
Prominin‐1 functions as an anchor for radixin, which brings PKA holoenzyme to membrane microdomains, where local cAMP concentration is increased by glucagon‐induced activation of adenylyl cyclase.
Prom1 knockout and knockdown result in inhibition of glucagon‐elicited CREB phosphorylation and gluconeogenesis in hepatocytes and livers.
Graphical Abstract
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.201949416</identifier><identifier>PMID: 33030802</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>A kinase-anchoring protein ; AC133 Antigen - genetics ; AC133 Antigen - metabolism ; Adenylate cyclase ; AMP ; Anchoring ; Animals ; cAMP signaling ; Cell surface ; Cyclic AMP ; Cyclic AMP response element-binding protein ; Cytoskeletal Proteins ; EMBO03 ; EMBO21 ; EMBO37 ; Epinephrine ; Forskolin ; Gene sequencing ; Glucagon ; Gluconeogenesis ; Gluconeogenesis - genetics ; Glucose - metabolism ; Hepatocytes ; Hyperglycemia ; Kinases ; Liver ; Liver - metabolism ; Membrane Proteins ; Membranes ; Mice ; Phosphorylation ; Prominin‐1 ; Protein kinase A ; Proteins ; Radixin ; Ribonucleic acid ; RNA ; Signaling ; Stem cell transplantation ; Stem cells ; Surface markers</subject><ispartof>EMBO reports, 2020-11, Vol.21 (11), p.e49416-n/a</ispartof><rights>The Author(s) 2020</rights><rights>2020 The Authors.</rights><rights>2020 EMBO</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5796-53a8f45b578d5799caee028e37432bfdcc97796f4420093e8f3b8e8ae85343ee3</citedby><cites>FETCH-LOGICAL-c5796-53a8f45b578d5799caee028e37432bfdcc97796f4420093e8f3b8e8ae85343ee3</cites><orcidid>0000-0002-8192-0946 ; 0000-0002-0969-2598</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/PMC7645247/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7645247/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27903,27904,41099,42168,45553,45554,46387,46811,51554,53769,53771</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.15252/embr.201949416$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33030802$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Hyun</creatorcontrib><creatorcontrib>Yu, Dong‐Min</creatorcontrib><creatorcontrib>Park, Jun Sub</creatorcontrib><creatorcontrib>Lee, Hwayeon</creatorcontrib><creatorcontrib>Kim, Jun‐Seok</creatorcontrib><creatorcontrib>Kim, Hong Lim</creatorcontrib><creatorcontrib>Koo, Seung‐Hoi</creatorcontrib><creatorcontrib>Lee, Jae‐Seon</creatorcontrib><creatorcontrib>Lee, Sungsoo</creatorcontrib><creatorcontrib>Ko, Young‐Gyu</creatorcontrib><title>Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>Prominin‐1 (Prom1) is a major cell surface marker of cancer stem cells, but its physiological functions in the liver have not been elucidated. We analyzed the levels of mRNA transcripts in serum‐starved primary WT (
Prom1
+/+
) and KO (
Prom1
−/−
) mouse hepatocytes using RNA sequencing (RNA‐seq) data, and found that CREB target genes were downregulated. This initial observation led us to determine that Prom1 deficiency inhibited cAMP response element‐binding protein (CREB) activation and gluconeogenesis, but not cyclic AMP (cAMP) accumulation, in glucagon‐, epinephrine‐, or forskolin‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐induced hyperglycemia. Because Prom1 interacted with radixin, Prom1 deficiency prevented radixin from localizing to the plasma membrane. Moreover, systemic adenoviral knockdown of radixin inhibited CREB activation and gluconeogenesis in glucagon‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐elicited hyperglycemia. Based on these results, we conclude that Prom1 regulates hepatic PKA signaling via radixin functioning as an A kinase‐anchored protein (AKAP).
Synopsis
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.
The transmembrane protein Prominin‐1 is expressed in hepatocytes as well as cholangiocytes in the liver.
Prominin‐1 functions as an anchor for radixin, which brings PKA holoenzyme to membrane microdomains, where local cAMP concentration is increased by glucagon‐induced activation of adenylyl cyclase.
Prom1 knockout and knockdown result in inhibition of glucagon‐elicited CREB phosphorylation and gluconeogenesis in hepatocytes and livers.
Graphical Abstract
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.</description><subject>A kinase-anchoring protein</subject><subject>AC133 Antigen - genetics</subject><subject>AC133 Antigen - metabolism</subject><subject>Adenylate cyclase</subject><subject>AMP</subject><subject>Anchoring</subject><subject>Animals</subject><subject>cAMP signaling</subject><subject>Cell surface</subject><subject>Cyclic AMP</subject><subject>Cyclic AMP response element-binding protein</subject><subject>Cytoskeletal Proteins</subject><subject>EMBO03</subject><subject>EMBO21</subject><subject>EMBO37</subject><subject>Epinephrine</subject><subject>Forskolin</subject><subject>Gene sequencing</subject><subject>Glucagon</subject><subject>Gluconeogenesis</subject><subject>Gluconeogenesis - genetics</subject><subject>Glucose - metabolism</subject><subject>Hepatocytes</subject><subject>Hyperglycemia</subject><subject>Kinases</subject><subject>Liver</subject><subject>Liver - metabolism</subject><subject>Membrane Proteins</subject><subject>Membranes</subject><subject>Mice</subject><subject>Phosphorylation</subject><subject>Prominin‐1</subject><subject>Protein kinase A</subject><subject>Proteins</subject><subject>Radixin</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Signaling</subject><subject>Stem cell transplantation</subject><subject>Stem cells</subject><subject>Surface markers</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9PFTEUxRuiAUTW7swkbtg86N-Z1oUJEAQjRkIguGs6fXeGkpn20c4gb-dH4DPySay-5xNNjIumze3vnpyTg9ArgneJoILuQV_HXYqJ4oqTcg1tEl6qCSOVfLZ8U0q-bKAXKd1gjIWq5DraYAwzLDHdRFdnMfTOO__47YHkc26m7t75wty7VNjghxi6VFzDzAzOFm035hmEFjykDNTzIkI7dvnTt8XZx_3C2MHduWH-Ej1vTJdge3lvocv3RxeHJ5PTz8cfDvdPJ1ZUqpwIZmTDRS0qOc0DZQ0AphJYxRmtm6m1qspcwznFWDGQDaslSANSMM4A2BZ6t9CdjXUPUwvZsen0LLrexLkOxuk_f7y71m2401XJBeVVFthZCsRwO0IadO-Sha4zOeeYNOVc0ZIRLjL65i_0JozR53iZygl4yRTO1N6CsjGkFKFZmSFY_yxN_yhNr0rLG6-fZljxv1rKwNsF8NV1MP-fnj76dHD-VB0vllPe8y3E367_Zeg7hg23AA</recordid><startdate>20201105</startdate><enddate>20201105</enddate><creator>Lee, Hyun</creator><creator>Yu, Dong‐Min</creator><creator>Park, Jun Sub</creator><creator>Lee, Hwayeon</creator><creator>Kim, Jun‐Seok</creator><creator>Kim, Hong Lim</creator><creator>Koo, Seung‐Hoi</creator><creator>Lee, Jae‐Seon</creator><creator>Lee, Sungsoo</creator><creator>Ko, Young‐Gyu</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</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>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8192-0946</orcidid><orcidid>https://orcid.org/0000-0002-0969-2598</orcidid></search><sort><creationdate>20201105</creationdate><title>Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity</title><author>Lee, Hyun ; Yu, Dong‐Min ; Park, Jun Sub ; Lee, Hwayeon ; Kim, Jun‐Seok ; Kim, Hong Lim ; Koo, Seung‐Hoi ; Lee, Jae‐Seon ; Lee, Sungsoo ; Ko, Young‐Gyu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5796-53a8f45b578d5799caee028e37432bfdcc97796f4420093e8f3b8e8ae85343ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>A kinase-anchoring protein</topic><topic>AC133 Antigen - genetics</topic><topic>AC133 Antigen - metabolism</topic><topic>Adenylate cyclase</topic><topic>AMP</topic><topic>Anchoring</topic><topic>Animals</topic><topic>cAMP signaling</topic><topic>Cell surface</topic><topic>Cyclic AMP</topic><topic>Cyclic AMP response element-binding protein</topic><topic>Cytoskeletal Proteins</topic><topic>EMBO03</topic><topic>EMBO21</topic><topic>EMBO37</topic><topic>Epinephrine</topic><topic>Forskolin</topic><topic>Gene sequencing</topic><topic>Glucagon</topic><topic>Gluconeogenesis</topic><topic>Gluconeogenesis - genetics</topic><topic>Glucose - metabolism</topic><topic>Hepatocytes</topic><topic>Hyperglycemia</topic><topic>Kinases</topic><topic>Liver</topic><topic>Liver - metabolism</topic><topic>Membrane Proteins</topic><topic>Membranes</topic><topic>Mice</topic><topic>Phosphorylation</topic><topic>Prominin‐1</topic><topic>Protein kinase A</topic><topic>Proteins</topic><topic>Radixin</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>Signaling</topic><topic>Stem cell transplantation</topic><topic>Stem cells</topic><topic>Surface markers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Hyun</creatorcontrib><creatorcontrib>Yu, Dong‐Min</creatorcontrib><creatorcontrib>Park, Jun Sub</creatorcontrib><creatorcontrib>Lee, Hwayeon</creatorcontrib><creatorcontrib>Kim, Jun‐Seok</creatorcontrib><creatorcontrib>Kim, Hong Lim</creatorcontrib><creatorcontrib>Koo, Seung‐Hoi</creatorcontrib><creatorcontrib>Lee, Jae‐Seon</creatorcontrib><creatorcontrib>Lee, Sungsoo</creatorcontrib><creatorcontrib>Ko, Young‐Gyu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</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_linktorsrc</fulltext></delivery><addata><au>Lee, Hyun</au><au>Yu, Dong‐Min</au><au>Park, Jun Sub</au><au>Lee, Hwayeon</au><au>Kim, Jun‐Seok</au><au>Kim, Hong Lim</au><au>Koo, Seung‐Hoi</au><au>Lee, Jae‐Seon</au><au>Lee, Sungsoo</au><au>Ko, Young‐Gyu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2020-11-05</date><risdate>2020</risdate><volume>21</volume><issue>11</issue><spage>e49416</spage><epage>n/a</epage><pages>e49416-n/a</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><abstract>Prominin‐1 (Prom1) is a major cell surface marker of cancer stem cells, but its physiological functions in the liver have not been elucidated. We analyzed the levels of mRNA transcripts in serum‐starved primary WT (
Prom1
+/+
) and KO (
Prom1
−/−
) mouse hepatocytes using RNA sequencing (RNA‐seq) data, and found that CREB target genes were downregulated. This initial observation led us to determine that Prom1 deficiency inhibited cAMP response element‐binding protein (CREB) activation and gluconeogenesis, but not cyclic AMP (cAMP) accumulation, in glucagon‐, epinephrine‐, or forskolin‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐induced hyperglycemia. Because Prom1 interacted with radixin, Prom1 deficiency prevented radixin from localizing to the plasma membrane. Moreover, systemic adenoviral knockdown of radixin inhibited CREB activation and gluconeogenesis in glucagon‐treated liver tissues and primary hepatocytes, and mitigated glucagon‐elicited hyperglycemia. Based on these results, we conclude that Prom1 regulates hepatic PKA signaling via radixin functioning as an A kinase‐anchored protein (AKAP).
Synopsis
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.
The transmembrane protein Prominin‐1 is expressed in hepatocytes as well as cholangiocytes in the liver.
Prominin‐1 functions as an anchor for radixin, which brings PKA holoenzyme to membrane microdomains, where local cAMP concentration is increased by glucagon‐induced activation of adenylyl cyclase.
Prom1 knockout and knockdown result in inhibition of glucagon‐elicited CREB phosphorylation and gluconeogenesis in hepatocytes and livers.
Graphical Abstract
Prominin‐1 in the hepatocytes interacts with radixin at the plasma membrane and regulates hepatic gluconeogenesis by augmenting PKA signaling via radixin as a PKA‐anchoring protein.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>33030802</pmid><doi>10.15252/embr.201949416</doi><tpages>21</tpages><orcidid>https://orcid.org/0000-0002-8192-0946</orcidid><orcidid>https://orcid.org/0000-0002-0969-2598</orcidid><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1469-221X |
| ispartof | EMBO reports, 2020-11, Vol.21 (11), p.e49416-n/a |
| issn | 1469-221X 1469-3178 |
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| source | Springer Nature OA Free Journals |
| subjects | A kinase-anchoring protein AC133 Antigen - genetics AC133 Antigen - metabolism Adenylate cyclase AMP Anchoring Animals cAMP signaling Cell surface Cyclic AMP Cyclic AMP response element-binding protein Cytoskeletal Proteins EMBO03 EMBO21 EMBO37 Epinephrine Forskolin Gene sequencing Glucagon Gluconeogenesis Gluconeogenesis - genetics Glucose - metabolism Hepatocytes Hyperglycemia Kinases Liver Liver - metabolism Membrane Proteins Membranes Mice Phosphorylation Prominin‐1 Protein kinase A Proteins Radixin Ribonucleic acid RNA Signaling Stem cell transplantation Stem cells Surface markers |
| title | Prominin‐1‐Radixin axis controls hepatic gluconeogenesis by regulating PKA activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T07%3A19%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_C6C&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Prominin%E2%80%901%E2%80%90Radixin%20axis%20controls%20hepatic%20gluconeogenesis%20by%20regulating%20PKA%20activity&rft.jtitle=EMBO%20reports&rft.au=Lee,%20Hyun&rft.date=2020-11-05&rft.volume=21&rft.issue=11&rft.spage=e49416&rft.epage=n/a&rft.pages=e49416-n/a&rft.issn=1469-221X&rft.eissn=1469-3178&rft_id=info:doi/10.15252/embr.201949416&rft_dat=%3Cproquest_C6C%3E2457846390%3C/proquest_C6C%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2457846390&rft_id=info:pmid/33030802&rfr_iscdi=true |