Ubiquitin-mediated degradation at the Golgi apparatus
- PMID: 37484530
- PMCID: PMC10357820
- DOI: 10.3389/fmolb.2023.1197921
Ubiquitin-mediated degradation at the Golgi apparatus
Abstract
The Golgi apparatus is an essential organelle of the secretory pathway in eukaryotic cells. It processes secretory and transmembrane proteins and orchestrates their transport to other endomembrane compartments or the plasma membrane. The Golgi apparatus thereby shapes the cell surface, controlling cell polarity, cell-cell communication, and immune signaling. The cytosolic face of the Golgi hosts and regulates signaling cascades, impacting most notably the DNA damage response and mitosis. These essential functions strongly depend on Golgi protein homeostasis and Golgi integrity. Golgi fragmentation and consequent malfunction is associated with neurodegenerative diseases and certain cancer types. Recent studies provide first insight into the critical role of ubiquitin signaling in maintaining Golgi integrity and in Golgi protein quality control. Similar to well described pathways at the endoplasmic reticulum, ubiquitin-dependent degradation of non-native proteins prevents the accumulation of toxic protein aggregates at the Golgi. Moreover, ubiquitination regulates Golgi structural rearrangements in response to cellular stress. Advances in elucidating ubiquitination and degradation events at the Golgi are starting to paint a picture of the molecular machinery underlying Golgi (protein) homeostasis.
Keywords: Golgi fragmentation; Golgi homeostasis; Golgi protein quality control; PROTAC; transmembrane protein degradation; ubiquitin E3 ligase; ubiquitin-mediated protein degradation.
Copyright © 2023 Buzuk and Hellerschmied.
Conflict of interest statement
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
Figures
![FIGURE 1](https://www.ncbi.nlm.nih.gov/pmc/articles/instance/10357820/bin/fmolb-10-1197921-g001.gif)
Similar articles
-
The E3 ubiquitin ligase MARCH2 regulates ERGIC3-dependent trafficking of secretory proteins.J Biol Chem. 2019 Jul 12;294(28):10900-10912. doi: 10.1074/jbc.RA119.007435. Epub 2019 May 29. J Biol Chem. 2019. PMID: 31142615 Free PMC article.
-
Ubiquitin-dependent and -independent proteasomal degradation of apoB associated with endoplasmic reticulum and Golgi apparatus, respectively, in HepG2 cells.J Cell Biochem. 2003 Aug 1;89(5):1019-29. doi: 10.1002/jcb.10538. J Cell Biochem. 2003. PMID: 12874835
-
Identification of candidate substrates for the Golgi Tul1 E3 ligase using quantitative diGly proteomics in yeast.Mol Cell Proteomics. 2014 Nov;13(11):2871-82. doi: 10.1074/mcp.M114.040774. Epub 2014 Jul 30. Mol Cell Proteomics. 2014. PMID: 25078903 Free PMC article.
-
Protein quality control at the Golgi.Curr Opin Cell Biol. 2022 Apr;75:102074. doi: 10.1016/j.ceb.2022.02.008. Epub 2022 Mar 29. Curr Opin Cell Biol. 2022. PMID: 35364487 Review.
-
How Is the Fidelity of Proteins Ensured in Terms of Both Quality and Quantity at the Endoplasmic Reticulum? Mechanistic Insights into E3 Ubiquitin Ligases.Int J Mol Sci. 2021 Feb 19;22(4):2078. doi: 10.3390/ijms22042078. Int J Mol Sci. 2021. PMID: 33669844 Free PMC article. Review.
Cited by
-
Targeting the Ubiquitin-Proteasome System and Recent Advances in Cancer Therapy.Cells. 2023 Dec 22;13(1):29. doi: 10.3390/cells13010029. Cells. 2023. PMID: 38201233 Free PMC article. Review.
References
-
- Bensimon A., Pizzagalli M. D., Kartnig F., Dvorak V., Essletzbichler P., Winter G. E., et al. (2020). Targeted degradation of SLC transporters reveals amenability of multi-pass transmembrane proteins to ligand-induced proteolysis. Cell Chem. Biol. 27 (6), 728–739.e9. 10.1016/j.chembiol.2020.04.003 - DOI - PMC - PubMed
Publication types
Grants and funding
LinkOut - more resources
Full Text Sources