ArticlePloS one2009
Identification and developmental expression of Xenopus laevis SUMO proteases.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Deciphering the cancer chemopreventive potential of phytochemicals: an integrative perspective on molecular targets and signaling networks.Cancer cell international · 2026Review
- SUMOylation of Psmd1 controls Adrm1 interaction with the proteasome.Cell reports · 2014Article
- Starting and stopping SUMOylation. What regulates the regulator?Chromosoma · 2013Review
- Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo.Cell reports · 2013Article
- SUMO2/3 modification of cyclin E contributes to the control of replication origin firing.Nature communications · 2013Article
- The biphasic redox sensing of SENP3 accounts for the HIF-1 transcriptional activity shift by oxidative stress.Acta pharmacologica Sinica · 2012Article
- The pharmacokinetics of enrofloxacin in adult African clawed frogs (Xenopus laevis).Journal of the American Association for Laboratory Animal Science : JAALAS · 2010Article
- Distribution and paralogue specificity of mammalian deSUMOylating enzymes.The Biochemical journal · 2010Article
- The fate of metaphase kinetochores is weighed in the balance of SUMOylation during S phase.Cell cycle (Georgetown, Tex.) · 2010Review
- The SUMO protease SENP6 is essential for inner kinetochore assembly.The Journal of cell biology · 2010Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
SUMO proteins are small ubiquitin-related modifiers. All SUMOs are synthesized as propeptides that are post-translationally cleaved prior to conjugation. After processing, SUMOs become covalently conjugated to cellular targets through a pathway that is similar to ubiquitination. Ubiquitin like protein proteases/Sentrin specific proteases (Ulp/SENPs) mediate both processing and deconjugation of SUMOs. The action of Ulp/SENPs makes SUMOylation a highly dynamic post-translational modification. To investigate how Ulp/SENPs are regulated in a developmental context, we isolated and characterized all Ulp/SENPs in Xenopus laevis. Xenopus possess homologues of mammalian SENP3, 5, 6 and 7. All of these enzymes reacted with HA-tagged vinyl sulfone derivatives of SUMO-2 (HA-SU2-VS) but not SUMO-1 (HA-SU1-VS), suggesting that they act primarily on SUMO-2 and -3. In contrast, Xenopus possess a single member of the SENP1/SENP2 subfamily of Ulp/SENPs, most closely related to mammalian SENP1. Xenopus SENP1 reacted with HA-SU1-VS and HA-SU2-VS, suggesting that it acts on all SUMO paralogues. We analyzed the mRNA and protein levels for each of the Ulp/SENPs through development; we found that they show distinct patterns of expression that may involve both transcriptional and post-transcriptional regulation. Finally, we have characterized the developmental function of the most abundant Ulp/SENP found within Xenopus eggs, SENP3. Depletion of SENP3 using morpholino antisense oligonucleotides (morpholinos) caused accumulation of high molecular weight SUMO-2/3 conjugated species, defects in developing embryos and changes in the expression of some genes regulated by the transforming growth factor beta (TGF-beta) pathway. These findings collectively indicate that SUMO proteases are both highly regulated and essential for normal development.
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