The Gid-complex: an emerging player in the ubiquitin ligase league
- PMID: 30893051
- DOI: 10.1515/hsz-2019-0139
The Gid-complex: an emerging player in the ubiquitin ligase league
Abstract
The Saccharomyces cerevisiae Gid-complex is a highly evolutionary conserved ubiquitin ligase with at least seven protein subunits. Here, we review our knowledge about the yeast Gid-complex as an important regulator of glucose metabolism, specifically targeting key enzymes of gluconeogenesis for degradation. Furthermore, we summarize existing data about the individual subunits, the topology and possible substrate recognition mechanisms and compare the striking similarities, but also differences, between the yeast complex and its vertebrate counterpart. Present data is summarized to give an overview about cellular processes regulated by the vertebrate GID-complex that range from cell cycle regulation, primary cilia function to the regulation of energy homeostasis. In conclusion, the vertebrate GID-complex evolved as a versatile ubiquitin ligase complex with functions beyond the regulation of glucose metabolism.
Keywords: CTLH-complex; cell cycle; energy homeostasis; metabolism; primary cilia; protein degradation.
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References
-
- Adams, J., Kelso, R., and Cooley, L. (2000). The kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol. 10, 17–24.
-
- Alibhoy, A.A., Giardina, B.J., Dunton, D.D., and Chiang, H.L. (2012). Vid30 is required for the association of Vid vesicles and actin patches in the vacuole import and degradation pathway. Autophagy 8, 29–46.
-
- Amerik, A., Swaminathan, S., Krantz, B.A., Wilkinson, K.D., and Hochstrasser, M. (1997). In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16, 4826–4838.
-
- Ammerer, G., Hunter, C.P., Rothman, J.H., Saari, G.C., Valls, L.A., and Stevens, T.H. (1986). PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell Biol. 6, 2490–2499.
-
- Angers, S., Thorpe, C.J., Biechele, T.L., Goldenberg, S.J., Zheng, N., MacCoss, M.J., and Moon, R.T. (2006). The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting dishevelled for degradation. Nat. Cell Biol. 8, 348–357.
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