Identification and developmental expression of Xenopus laevis SUMO proteases.
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 prote...
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Public Library of Science (PLoS)
2009-12-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2794540?pdf=render |
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author | Yonggang Wang Debaditya Mukhopadhyay Smita Mathew Takashi Hasebe Rachel A Heimeier Yoshiaki Azuma Nagamalleswari Kolli Yun-Bo Shi Keith D Wilkinson Mary Dasso |
author_facet | Yonggang Wang Debaditya Mukhopadhyay Smita Mathew Takashi Hasebe Rachel A Heimeier Yoshiaki Azuma Nagamalleswari Kolli Yun-Bo Shi Keith D Wilkinson Mary Dasso |
author_sort | Yonggang Wang |
collection | DOAJ |
description | 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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spelling | doaj.art-41ec5bb683184ea0bbd3c5895652629a2022-12-22T00:48:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-12-01412e846210.1371/journal.pone.0008462Identification and developmental expression of Xenopus laevis SUMO proteases.Yonggang WangDebaditya MukhopadhyaySmita MathewTakashi HasebeRachel A HeimeierYoshiaki AzumaNagamalleswari KolliYun-Bo ShiKeith D WilkinsonMary DassoSUMO 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.http://europepmc.org/articles/PMC2794540?pdf=render |
spellingShingle | Yonggang Wang Debaditya Mukhopadhyay Smita Mathew Takashi Hasebe Rachel A Heimeier Yoshiaki Azuma Nagamalleswari Kolli Yun-Bo Shi Keith D Wilkinson Mary Dasso Identification and developmental expression of Xenopus laevis SUMO proteases. PLoS ONE |
title | Identification and developmental expression of Xenopus laevis SUMO proteases. |
title_full | Identification and developmental expression of Xenopus laevis SUMO proteases. |
title_fullStr | Identification and developmental expression of Xenopus laevis SUMO proteases. |
title_full_unstemmed | Identification and developmental expression of Xenopus laevis SUMO proteases. |
title_short | Identification and developmental expression of Xenopus laevis SUMO proteases. |
title_sort | identification and developmental expression of xenopus laevis sumo proteases |
url | http://europepmc.org/articles/PMC2794540?pdf=render |
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