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Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation
Stockholm University, Faculty of Science, The Wenner-Gren Institute .
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2011 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 585, no 24, 3856-3861 p.Article in journal (Refereed) Published
Abstract [en]

The two major antagonistic pathways of carbon metabolism in cells, glycolysis and gluconeogenesis, are tightly regulated. In the eukaryotic model organism Saccharomyces cerevisiae the switch from gluconeogenesis to glycolysis is brought about by proteasomal degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase. The ubiquitin ligase responsible for polyubiquitylation of fructose-1,6-bisphosphatase is the Gid complex. This complex consists of seven subunits of which subunit Gid2/Rmd5 contains a RING finger domain providing E3 ligase activity. Here we identify an additional subunit containing a degenerated RING finger, Gid9/Fyv10. This subunit binds to Gid2/Rmd5. A mutation in the degenerated RING finger of Gid9/Fyv10 abolishes polyubiquitylation and degradation of three enzymes specific for gluconeogenesis. Structured summary of protein interactions: Gid2 physically interacts with Gid9 by anti tag coimmunoprecipitation (View interaction) (C) 2011 Federation of European Biochemical Societies.

Place, publisher, year, edition, pages
2011. Vol. 585, no 24, 3856-3861 p.
Keyword [en]
Catabolite degradation, Gid ubiquitin ligase, RING finger, Glycolysis, Gluconeogenesis, Fructose-1, 6-bisphosphatase
National Category
Natural Sciences
URN: urn:nbn:se:su:diva-71147DOI: 10.1016/j.febslet.2011.10.038ISI: 000298133300003OAI: diva2:483925
authorCount :6Available from: 2012-01-26 Created: 2012-01-26 Last updated: 2012-01-26Bibliographically approved

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