publication . Other literature type . Article . 2008

The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.

Olivier Santt; Thorsten Pfirrmann; Bernhard Braun; Jeannette Juretschke; Philipp Kimmig; Hartmut Scheel; Kay Hofmann; Michael Thumm; Dieter H. Wolf;
Open Access English
  • Published: 01 Aug 2008
  • Publisher: The American Society for Cell Biology
Abstract
<jats:p>Glucose-dependent regulation of carbon metabolism is a subject of intensive studies. We have previously shown that the switch from gluconeogenesis to glycolysis is associated with ubiquitin-proteasome linked elimination of the key enzyme fructose-1,6-bisphosphatase. Seven glucose induced degradation deficient (Gid)-proteins found previously in a genomic screen were shown to form a complex that binds FBPase. One of the subunits, Gid2/Rmd5, contains a degenerated RING finger domain. In an in vitro assay, heterologous expression of GST-Gid2 leads to polyubiquitination of proteins. In addition, we show that a mutation in the degenerated RING domain of Gid2/R...
Subjects
free text keywords: Articles, Cell Biology, Molecular Biology
Abstract
<jats:p>Glucose-dependent regulation of carbon metabolism is a subject of intensive studies. We have previously shown that the switch from gluconeogenesis to glycolysis is associated with ubiquitin-proteasome linked elimination of the key enzyme fructose-1,6-bisphosphatase. Seven glucose induced degradation deficient (Gid)-proteins found previously in a genomic screen were shown to form a complex that binds FBPase. One of the subunits, Gid2/Rmd5, contains a degenerated RING finger domain. In an in vitro assay, heterologous expression of GST-Gid2 leads to polyubiquitination of proteins. In addition, we show that a mutation in the degenerated RING domain of Gid2/R...
Subjects
free text keywords: Articles, Cell Biology, Molecular Biology
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