Regulation of the Gid ubiquitin ligase recognition subunit Gid4

Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are devoid of glucose. Availability of glucose immedi...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 2018-10, Vol.592 (19), p.3286-3294
Main Authors: Menssen, Ruth, Bui, Kim, Wolf, Dieter H.
Format: Article
Language:English
Subjects:
catabolite‐induced degradation
Gid ubiquitin ligase
Gid4
gluconeogenic enzymes
glucose metabolism
ubiquitin proteasome system
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873
cites cdi_FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873
container_end_page 3294
container_issue 19
container_start_page 3286
container_title FEBS letters
container_volume 592
creator Menssen, Ruth
Bui, Kim
Wolf, Dieter H.
description Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are devoid of glucose. Availability of glucose immediately leads to inactivation and rapid degradation of these enzymes via the ubiquitin proteasome system. Polyubiquitination is carried out by the Gid complex, a multisubunit RING E3 ligase that constitutively consists of six different proteins. Upon addition of glucose to the medium, the substrate recognition subunit Gid4 appears within minutes and triggers ubiquitination of the gluconeogenic enzymes. Here, we show that Gid4 is tightly regulated on the transcriptional and protein level to ensure proper adjustment of gluconeogenesis.
doi_str_mv 10.1002/1873-3468.13229
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2092534890</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2092534890</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873</originalsourceid><addsrcrecordid>eNqFkM1LwzAYh4Mobk7P3qRHL93y1TY5iY5tCgNB9BzS9O2MdO3WNMj-e9N1evX0fvC8P3gfhG4JnhKM6YyIjMWMp2JKGKXyDI3_NudojDHhcZJJNkJXzn3hMAsiL9GIYcJSRrIxeniDja90Z5s6asqo-4RoZYvI53bvbWfrqLIb7SBqwTSb2h4553Mf2h7k1-ii1JWDm1OdoI_l4n3-HK9fVy_zx3VsGOcylpkAbowAU2hRpkKXRuSlLrkuUig4gE6YoXmepzTsM5YbqSEpUkYDmoSXJuh-yN21zd6D69TWOgNVpWtovFMUS5owLiQO6GxATds410Kpdq3d6vagCFa9NdU7Ur0jdbQWLu5O4T7fQvHH_2oKQDoA37aCw395arl4okPyDyhtd8g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2092534890</pqid></control><display><type>article</type><title>Regulation of the Gid ubiquitin ligase recognition subunit Gid4</title><source>Wiley-Blackwell Read &amp; Publish Collection</source><creator>Menssen, Ruth ; Bui, Kim ; Wolf, Dieter H.</creator><creatorcontrib>Menssen, Ruth ; Bui, Kim ; Wolf, Dieter H.</creatorcontrib><description>Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are devoid of glucose. Availability of glucose immediately leads to inactivation and rapid degradation of these enzymes via the ubiquitin proteasome system. Polyubiquitination is carried out by the Gid complex, a multisubunit RING E3 ligase that constitutively consists of six different proteins. Upon addition of glucose to the medium, the substrate recognition subunit Gid4 appears within minutes and triggers ubiquitination of the gluconeogenic enzymes. Here, we show that Gid4 is tightly regulated on the transcriptional and protein level to ensure proper adjustment of gluconeogenesis.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.13229</identifier><identifier>PMID: 30136317</identifier><language>eng</language><publisher>England</publisher><subject>catabolite‐induced degradation ; Gid ubiquitin ligase ; Gid4 ; gluconeogenic enzymes ; glucose metabolism ; ubiquitin proteasome system</subject><ispartof>FEBS letters, 2018-10, Vol.592 (19), p.3286-3294</ispartof><rights>2018 Federation of European Biochemical Societies</rights><rights>2018 Federation of European Biochemical Societies.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873</citedby><cites>FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27900,27901</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30136317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Menssen, Ruth</creatorcontrib><creatorcontrib>Bui, Kim</creatorcontrib><creatorcontrib>Wolf, Dieter H.</creatorcontrib><title>Regulation of the Gid ubiquitin ligase recognition subunit Gid4</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are devoid of glucose. Availability of glucose immediately leads to inactivation and rapid degradation of these enzymes via the ubiquitin proteasome system. Polyubiquitination is carried out by the Gid complex, a multisubunit RING E3 ligase that constitutively consists of six different proteins. Upon addition of glucose to the medium, the substrate recognition subunit Gid4 appears within minutes and triggers ubiquitination of the gluconeogenic enzymes. Here, we show that Gid4 is tightly regulated on the transcriptional and protein level to ensure proper adjustment of gluconeogenesis.</description><subject>catabolite‐induced degradation</subject><subject>Gid ubiquitin ligase</subject><subject>Gid4</subject><subject>gluconeogenic enzymes</subject><subject>glucose metabolism</subject><subject>ubiquitin proteasome system</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkM1LwzAYh4Mobk7P3qRHL93y1TY5iY5tCgNB9BzS9O2MdO3WNMj-e9N1evX0fvC8P3gfhG4JnhKM6YyIjMWMp2JKGKXyDI3_NudojDHhcZJJNkJXzn3hMAsiL9GIYcJSRrIxeniDja90Z5s6asqo-4RoZYvI53bvbWfrqLIb7SBqwTSb2h4553Mf2h7k1-ii1JWDm1OdoI_l4n3-HK9fVy_zx3VsGOcylpkAbowAU2hRpkKXRuSlLrkuUig4gE6YoXmepzTsM5YbqSEpUkYDmoSXJuh-yN21zd6D69TWOgNVpWtovFMUS5owLiQO6GxATds410Kpdq3d6vagCFa9NdU7Ur0jdbQWLu5O4T7fQvHH_2oKQDoA37aCw395arl4okPyDyhtd8g</recordid><startdate>201810</startdate><enddate>201810</enddate><creator>Menssen, Ruth</creator><creator>Bui, Kim</creator><creator>Wolf, Dieter H.</creator><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201810</creationdate><title>Regulation of the Gid ubiquitin ligase recognition subunit Gid4</title><author>Menssen, Ruth ; Bui, Kim ; Wolf, Dieter H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>catabolite‐induced degradation</topic><topic>Gid ubiquitin ligase</topic><topic>Gid4</topic><topic>gluconeogenic enzymes</topic><topic>glucose metabolism</topic><topic>ubiquitin proteasome system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Menssen, Ruth</creatorcontrib><creatorcontrib>Bui, Kim</creatorcontrib><creatorcontrib>Wolf, Dieter H.</creatorcontrib><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>Menssen, Ruth</au><au>Bui, Kim</au><au>Wolf, Dieter H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of the Gid ubiquitin ligase recognition subunit Gid4</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2018-10</date><risdate>2018</risdate><volume>592</volume><issue>19</issue><spage>3286</spage><epage>3294</epage><pages>3286-3294</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Glucose consumption via glycolysis and its biosynthesis via gluconeogenesis are central reciprocal pathways controlled by a set of different enzymes. In the yeast Saccharomyces cerevisiae, expression of gluconeogenic enzymes is induced when cells are devoid of glucose. Availability of glucose immediately leads to inactivation and rapid degradation of these enzymes via the ubiquitin proteasome system. Polyubiquitination is carried out by the Gid complex, a multisubunit RING E3 ligase that constitutively consists of six different proteins. Upon addition of glucose to the medium, the substrate recognition subunit Gid4 appears within minutes and triggers ubiquitination of the gluconeogenic enzymes. Here, we show that Gid4 is tightly regulated on the transcriptional and protein level to ensure proper adjustment of gluconeogenesis.</abstract><cop>England</cop><pmid>30136317</pmid><doi>10.1002/1873-3468.13229</doi><tpages>9</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0014-5793
ispartof FEBS letters, 2018-10, Vol.592 (19), p.3286-3294
issn 0014-5793
1873-3468
language eng
recordid cdi_proquest_miscellaneous_2092534890
source Wiley-Blackwell Read & Publish Collection
subjects catabolite‐induced degradation
Gid ubiquitin ligase
Gid4
gluconeogenic enzymes
glucose metabolism
ubiquitin proteasome system
title Regulation of the Gid ubiquitin ligase recognition subunit Gid4
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-25T11%3A28%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20the%20Gid%20ubiquitin%20ligase%20recognition%20subunit%20Gid4&rft.jtitle=FEBS%20letters&rft.au=Menssen,%20Ruth&rft.date=2018-10&rft.volume=592&rft.issue=19&rft.spage=3286&rft.epage=3294&rft.pages=3286-3294&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1002/1873-3468.13229&rft_dat=%3Cproquest_cross%3E2092534890%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3449-978e4cc8ecda8f68afc8bfaf4ad6ed4eea53c2bbb628bf73bc9ae5d6328af5873%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2092534890&rft_id=info:pmid/30136317&rfr_iscdi=true