ArticleThe Journal of biological chemistry2012
Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- UBA2: the gatekeeper of the sumoylation pathway and its multifaceted roles in human diseases and therapeutic prospects.Clinical and experimental medicine · 2026Review
- Structural insights into the regulation of the human E2∼SUMO conjugate through analysis of its stable mimetic.The Journal of biological chemistry · 2023Article
- SUMOylation Wrestles With the Occurrence and Development of Breast Cancer.Frontiers in oncology · 2021Review
- The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells.PLoS pathogens · 2020Article
- The Function of SUMOylation and Its Role in the Development of Cancer Cells under Stress Conditions: A Systematic Review.Stem cells international · 2020Review
- The ubiquitin-like modifier FAT10 interferes with SUMO activation.Nature communications · 2019Article
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
- DENEDDYLASE1 Protein Counters Automodification of Neddylating Enzymes to Maintain NEDD8 Protein Homeostasis inThe Journal of biological chemistry · 2017Article
- SUMO and the robustness of cancer.Nature reviews. Cancer · 2017Review
- Sulfur transfer and activation by ubiquitin-like modifier system Uba4•Urm1 link protein urmylation and tRNA thiolation in yeast.Microbial cell (Graz, Austria) · 2016Article
- Mechanistic insight into protein modification and sulfur mobilization activities of noncanonical E1 and associated ubiquitin-like proteins of Archaea.The FEBS journal · 2016Article
- Is Transthyretin a Regulator of Ubc9 SUMOylation?PloS one · 2016Article
- RWD Domain as an E2 (Ubc9)-Interaction Module.The Journal of biological chemistry · 2015Article
- Article
- Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Physiological reviews · 2014Review
- Ehrlichia chaffeensis exploits host SUMOylation pathways to mediate effector-host interactions and promote intracellular survival.Infection and immunity · 2014Article
- Synthesis of 2',3',4'-trihydroxyflavone (2-D08), an inhibitor of protein sumoylation.Bioorganic & medicinal chemistry letters · 2014Article
- SUMO rules: regulatory concepts and their implication in neurologic functions.Neuromolecular medicine · 2013Review
- Starting and stopping SUMOylation. What regulates the regulator?Chromosoma · 2013Review
- Sumoylation of SAE2 C terminus regulates SAE nuclear localization.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Although it is well established that ubiquitin-like modifications are tightly regulated, it has been unclear how their E1 activities are controlled. In this study, we found that the SAE2 subunit of the small ubiquitin-like modifier (SUMO) E1 is autoSUMOylated at residue Lys-236, and SUMOylation was catalyzed by Ubc9 at several additional Lys residues surrounding the catalytic Cys-173 of SAE2. AutoSUMOylation of SAE2 did not affect SUMO adenylation or formation of E1·SUMO thioester, but did significantly inhibit the transfer of SUMO from E1 to E2 and overall SUMO conjugations to target proteins due to the altered interaction between E1 and E2. Upon heat shock, SUMOylation of SAE2 was reduced, which corresponded with an increase in global SUMOylation, suggesting that SUMOylation of the Cys domain of SAE2 is a mechanism for "storing" a pool of E1 that can be quickly activated in response to environmental changes. This study is the first to show how E1 activity is controlled by post-translational modifications, and similar regulation likely exists across the homologous E1s of ubiquitin-like modifications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.