» Articles » PMID: 20159987

Ubiquitin Chain Elongation Enzyme Ufd2 Regulates a Subset of Doa10 Substrates

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2010 Feb 18
PMID 20159987
Citations 19
Authors
Affiliations
Soon will be listed here.
Abstract

Ufd2 is the founding member of E4 enzymes that are specifically involved in ubiquitin chain elongation but whose roles in proteolysis remain scarce. Here, using a genome-wide screen, we identified one cellular target of yeast Ufd2 as the membrane protein Pex29. The ubiquitin chains assembled on Pex29 in vivo by Ufd2 mainly contain Lys-48 linkages. We found that the ubiquitin-protein E3 ligase for overexpressed Pex29 is Doa10, which is known to be involved in protein quality control. Interestingly, not all Doa10 substrates are regulated by Ufd2, suggesting that E4 involvement is not specific to a particular E3, but may depend on the spatial arrangement of the E3-substrate interaction. Cells lacking UFD2 elicit an unfolded protein response, expanding the physiological function of Ufd2. Our results lead to novel insights into the biological role of Ufd2 and further underscore the significance of Ufd2 in proteolysis.

Citing Articles

The Dsc complex and its role in Golgi quality control.

Weyer Y, Teis D Biochem Soc Trans. 2024; 52(5):2023-2034.

PMID: 39324639 PMC: 11555709. DOI: 10.1042/BST20230375.


Pin1-Catalyzed Conformation Changes Regulate Protein Ubiquitination and Degradation.

Jeong J, Usman M, Li Y, Zhou X, Lu K Cells. 2024; 13(9.

PMID: 38727267 PMC: 11083468. DOI: 10.3390/cells13090731.


E4 ubiquitin ligase promotes mitofusin turnover and mitochondrial stress response.

Anton V, Buntenbroich I, Simoes T, Joaquim M, Muller L, Buettner R Mol Cell. 2023; 83(16):2976-2990.e9.

PMID: 37595558 PMC: 10434984. DOI: 10.1016/j.molcel.2023.07.021.


Ubiquitination in the ERAD Process.

Lopata A, Kniss A, Lohr F, Rogov V, Dotsch V Int J Mol Sci. 2020; 21(15).

PMID: 32731622 PMC: 7432864. DOI: 10.3390/ijms21155369.


Ubiquitin-dependent protein degradation at the endoplasmic reticulum and nuclear envelope.

Mehrtash A, Hochstrasser M Semin Cell Dev Biol. 2018; 93:111-124.

PMID: 30278225 PMC: 6748311. DOI: 10.1016/j.semcdb.2018.09.013.


References
1.
Apodaca J, Kim I, Rao H . Cellular tolerance of prion protein PrP in yeast involves proteolysis and the unfolded protein response. Biochem Biophys Res Commun. 2006; 347(1):319-26. DOI: 10.1016/j.bbrc.2006.06.078. View

2.
Hosoda M, Ozaki T, Miyazaki K, Hayashi S, Furuya K, Watanabe K . UFD2a mediates the proteasomal turnover of p73 without promoting p73 ubiquitination. Oncogene. 2005; 24(48):7156-69. DOI: 10.1038/sj.onc.1208872. View

3.
Hoppe T, Cassata G, Barral J, Springer W, Hutagalung A, Epstein H . Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans. Cell. 2004; 118(3):337-49. DOI: 10.1016/j.cell.2004.07.014. View

4.
Hanna J, Finley D . A proteasome for all occasions. FEBS Lett. 2007; 581(15):2854-61. PMC: 1965587. DOI: 10.1016/j.febslet.2007.03.053. View

5.
Measday V, Hieter P . Synthetic dosage lethality. Methods Enzymol. 2002; 350:316-26. DOI: 10.1016/s0076-6879(02)50971-x. View