ArticleMolecular biology of the cell2008
Different domains of the UBL-UBA ubiquitin receptor, Ddi1/Vsm1, are involved in its multiple cellular roles.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 59 citations in OpenAlex.
- Domains in Action: Understanding Ddi1's Diverse Functions in the Ubiquitin-Proteasome System.International journal of molecular sciences · 2024Review
- Proteasome condensate formation is driven by multivalent interactions with shuttle factors and ubiquitin chains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The ubiquitin-binding protein MdRAD23D1 mediates drought response by regulating degradation of the proline-rich protein MdPRP6 in apple (Malus domestica).Plant biotechnology journal · 2023Article
- Structural and functional insights into the DNA damage-inducible protein 1 (Ddi1) from protozoa.Current research in structural biology · 2022Article
- Article
- Weighted miRNA co-expression network reveals potential roles of apoptosis related pathways and crucial genes in thoracic aortic aneurysm.Journal of thoracic disease · 2021Article
- Wss1 homolog from Candida albicans and its role in DNA-protein crosslink tolerance.Molecular microbiology · 2020Article
- DDI2 Is a Ubiquitin-Directed Endoprotease Responsible for Cleavage of Transcription Factor NRF1.Molecular cell · 2020Article
- Malaria parasite plasmepsins: More than just plain old degradative pepsins.The Journal of biological chemistry · 2020Review
- Ddi1 is a ubiquitin-dependent protease.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dimer Interface Organization is a Main Determinant of Intermonomeric Interactions and Correlates with Evolutionary Relationships of Retroviral and Retroviral-Like Ddi1 and Ddi2 Proteases.International journal of molecular sciences · 2020Article
- Disabling the Protease DDI2 Attenuates the Transcriptional Activity of NRF1 and Potentiates Proteasome Inhibitor Cytotoxicity.International journal of molecular sciences · 2020Article
- Non-Proteasomal UbL-UbA Family of Proteins in Neurodegeneration.International journal of molecular sciences · 2019Review
- Review
- Crystal structure of the retroviral protease-like domain of a protozoal DNA damage-inducible 1 protein.FEBS open bio · 2018Article
- Cdc48 and ubiquilins confer selective anterograde protein sorting and entry into the multivesicular body in yeast.Molecular biology of the cell · 2018Article
- Article
- ERG-28 controls BK channel trafficking in the ER to regulate synaptic function and alcohol response ineLife · 2017Article
- Up-regulated NRIP2 in colorectal cancer initiating cells modulates the Wnt pathway by targeting RORβ.Molecular cancer · 2017Article
- Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Scientific reports · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ddi1/Vsm1 is an ubiquitin receptor involved in regulation of the cell cycle and late secretory pathway in Saccharomyces cerevisiae. Ddi1 possesses three domains: an NH(2)-terminal ubiquitin-like domain (UBL), a COOH-terminal ubiquitin-associated domain (UBA), and a retroviral aspartyl-protease domain (RVP). Here, we demonstrate the domains involved in homodimerization, checkpoint regulation, localization, and t-SNARE binding. The RVP domain is required for protein homodimerization, whereas the UBL and UBA domains are required for rescue of the pds1-128 checkpoint mutant and enrichment of GFP-Ddi1 in the nucleus. A mutation in aspartate-220, which is necessary for putative aspartyl-protease function, abolished the rescue of pds1-128 cells but not homodimerization. Thus, Ddi1 catalytic activity may be required for checkpoint regulation. The Sso1 t-SNARE-interacting domain maps to residues 344-395 and undergoes phosphorylation on threonines T346 and T348. T348 is necessary for Sso binding, and phosphorylation is important for function, because mutations that lessen phosphorylation (e.g., Ddi1(T346A), Ddi1(T348A)) are unable to facilitate growth of the sec9-4 t-SNARE mutant. In contrast, the overproduction of phosphorylatable forms of Ddi1 (e.g., Ddi1, Ddi1(S341A)) rescue the growth of sec9-4 cells similar to Sso1 overproduction. Thus, Ddi1 participates in multiple cellular processes via its different domains and phosphorylation may regulate exocytic functions.
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