The DOI matches its Crossref record.
The Sumo protease Senp7 is required for proper neuronal differentiation
Open accessAbstract
Covalent attachment of the Small ubiquitin-like modifier (Sumo) polypeptide to proteins regulates many processes in the eukaryotic cell. In the nervous system, Sumo has been associated with the synapsis and with neurodegenerative diseases. However, its involvement in regulating neuronal differentiation remains largely unknown. Here we show that net Sumo deconjugation is observed during neurogenesis and that Sumo overexpression impairs this process. In an attempt to shed light on the underlying mechanisms, we have analyzed the expression profile of genes coding for components of the sumoylation pathway following induction of neuronal differentiation. Interestingly, we observed strong upregulation of the Senp7 protease at both mRNA and protein levels under differentiation conditions. Sumo proteases, by removing Sumo from targets, are key regulators of sumoylation. Strikingly, loss-of-function analysis demonstrated that Senp7 is required for neuronal differentiation not only in a model cell line, but also in the developing neural tube. Finally, reporter-based analysis of the Senp7 promoter indicated that Senp7 was transiently activated at early stages of neuronal differentiation. Thus, the Sumo protease Senp7 adds to the list of factors involved in vertebrate neurogenesis.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Furthermore, recent whole blood and cell-specific Methylome-wide association studies (MWAS) from a sample of adolescents with CU disorder pointed at many methylation sites relevant to brain function and to neurodevelopment (Clark et al., 2021). These included CpGs located in the CLMN gene and the SENP7 gene, expressed in the brain and playing a role in brain developmental and synaptic function and”
From Can epigenetics shine a light on the biological pathways underlying major mental disorders? (2022) · cites this paper as Juarez-Vicente, Luna-Pelaez, & Garcia-Dominguez, 2016
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
No references could be resolved yet.
Research works printed but not linked: 34
- Huang, 2014, Proneural bHLH genes in development and disease, Curr. Top. Dev. Biol., 110, 75, 10.1016/B978-0-12-405943-6.00002-6 · DOI
- Urban, 2014, Neurogenesis in the embryonic and adult brain: same regulators, different roles, Front. Cell. Neurosci., 8, 396, 10.3389/fncel.2014.00396 · DOI · Paper page
- Flotho, 2013, Sumoylation: a regulatory protein modification in health and disease, Annu. Rev. Biochem., 82, 357, 10.1146/annurev-biochem-061909-093311 · DOI
- Garcia-Dominguez, 2009, SUMO association with repressor complexes, emerging routes for transcriptional control, Biochim. Biophys. Acta, 1789, 451, 10.1016/j.bbagrm.2009.07.001 · DOI
- Tempe, 2008, SUMO under stress, Biochem. Soc. Trans., 36, 874, 10.1042/BST0360874 · DOI
- Hay, 2005, SUMO: a history of modification, Mol. Cell, 18, 1, 10.1016/j.molcel.2005.03.012 · DOI
- Mukhopadhyay, 2007, Modification in reverse: the SUMO proteases, Trends Biochem. Sci., 32, 286, 10.1016/j.tibs.2007.05.002 · DOI
- Shin, 2012, DeSUMOylating isopeptidase: a second class of SUMO protease, EMBO Rep., 13, 339, 10.1038/embor.2012.3 · DOI
- Yeh, 2009, SUMOylation and De-SUMOylation: wrestling with life's processes, J. Biol. Chem., 284, 8223, 10.1074/jbc.R800050200 · DOI
- Gwizdek, 2013, Protein sumoylation in brain development, neuronal morphology and spinogenesis, Neruomol. Med., 15, 677, 10.1007/s12017-013-8252-z · DOI
- Henley, 2014, Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction, Physiol. Rev., 94, 1249, 10.1152/physrev.00008.2014 · DOI
- Garcia-Gutierrez, 2011, The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators, EMBO Rep., 12, 1018, 10.1038/embor.2011.152 · DOI
- Giudicelli, 2003, Novel activities of Mafb underlie its dual role in hindbrain segmentation and regional specification, Dev. Biol., 253, 150, 10.1006/dbio.2002.0864 · DOI
- Farah, 2000, Generation of neurons by transient expression of neural bHLH proteins in mammalian cells, Development, 127, 693, 10.1242/dev.127.4.693 · DOI
- Garcia-Dominguez, 2003, Ebf gene function is required for coupling neuronal differentiation and cell cycle exit, Development, 130, 6013, 10.1242/dev.00840 · DOI
- Garcia-Gutierrez, 2014, Pleiotrophin antagonizes Brd2 during neuronal differentiation, J. Cell Sci., 127, 2554
- Sharma, 2013, Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo, Cell Rep., 3, 1640, 10.1016/j.celrep.2013.04.016 · DOI
- Pfaffl, 2001, A new mathematical model for relative quantification in real-time RT-PCR, Nucleic Acids Res., 29, 10.1093/nar/29.9.e45 · DOI · Paper page
- McBurney, 1993, P19 embryonal carcinoma cells, Int. J. Dev. Biol., 37, 135, 10.1387/ijdb.8507558 · DOI
- Garcia-Gutierrez, 2012, Association of bromodomain BET proteins with chromatin requires dimerization through the conserved motif B, J. Cell Sci., 125, 3671, 10.1242/jcs.105841 · DOI
- Ma, 1999, Neurogenin1 and neurogenin2 control two distinct waves of neurogenesis in developing dorsal root ganglia, Genes Dev., 13, 1717, 10.1101/gad.13.13.1717 · DOI
- Perez, 1999, Early specification of sensory neuron fate revealed by expression and function of neurogenins in the chick embryo, Development, 126, 1715, 10.1242/dev.126.8.1715 · DOI
- Roztocil, 1997, NeuroM, a neural helix-loop-helix transcription factor, defines a new transition stage in neurogenesis, Development, 124, 3263, 10.1242/dev.124.17.3263 · DOI
- Hasegawa, 2014, Spatiotemporal distribution of SUMOylation components during mouse brain development, J. Comp. Neurol., 522, 3020, 10.1002/cne.23563 · DOI
- Loriol, 2012, Developmental regulation and spatiotemporal redistribution of the sumoylation machinery in the rat central nervous system, PLoS One, 7, 10.1371/journal.pone.0033757 · DOI
- Watanabe, 2008, Developmental regulation of Ubc9 in the rat nervous system, Acta Biochim. Pol., 55, 681, 10.18388/abp.2008_3027 · DOI
- Ceballos-Chavez, 2012, Control of neuronal differentiation by sumoylation of BRAF35, a subunit of the LSD1-CoREST histone demethylase complex, Proc. Natl. Acad. Sci. U. S. A., 109, 8085, 10.1073/pnas.1121522109 · DOI
- Di Bacco, 2006, The SUMO-specific protease SENP5 is required for cell division, Mol. Cell. Biol., 26, 4489, 10.1128/MCB.02301-05 · DOI
- Gong, 2006, Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3, J. Biol. Chem., 281, 15869, 10.1074/jbc.M511658200 · DOI
- Shen, 2009, Characterization of SENP7, a SUMO-2/3-specific isopeptidase, Biochem. J., 421, 223, 10.1042/BJ20090246 · DOI
- Maison, 2012, The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin, Nat. Struct. Mol. Biol., 19, 458, 10.1038/nsmb.2244 · DOI
- Romeo, 2015, The SENP7 SUMO-Protease Presents a Module of two HP1 Interaction Motifs that Locks HP1 protein at pericentric heterochromatin, Cell Rep., 10.1016/j.celrep.2015.01.004 · DOI
- Federzoni, 2015, Linking the SUMO protease SENP5 to neutrophil differentiation of AML cells, Leuk. Res. Rep., 4, 32
- Ma, 1996, Identification of neurogenin, a vertebrate neuronal determination gene, Cell, 87, 43, 10.1016/S0092-8674(00)81321-5 · DOI
Cited by
Sorted by citations
Protein SUMOylation modification and its associations with disease
Yang, Y., He, Y., Wang, X., liang, Z., He, G., Zhang, P., Zhu, H., Xu, N., & Liang, S. (2017) · Open Biology · doi:10.1098/rsob.170167 · Cited by 216
Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts
Celen, A. B., & Şahin, U. (2020) · FEBS Journal · doi:10.1111/febs.15319 · Cited by 255
Sumoylation in Physiology, Pathology and Therapy
Şahin, U., de Thé, H., & Lallemand-Breitenbach, V. (2022) · Cells · doi:10.3390/cells11050814 · Cited by 100
Can epigenetics shine a light on the biological pathways underlying major mental disorders?
Alameda, L., Trotta, G., Quigley, H., Rodriguez, V., Gadelrab, R., Dwir, D., Dempster, E., Wong, C. C. Y., & Forti, M. D. (2022) · Psychological Medicine · doi:10.1017/s0033291721005559 · Cited by 60
The role of SUMOylation during development
Talamillo, A., Barroso-Gomila, O., Giordano, I., Ajuria, L., Grillo, M., Mayor, U., & Barrio, R. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190390 · Cited by 43
Metadata
- Authors
- Juarez-Vicente, F., Luna-Pelaez, N., & Garcia-Dominguez, M.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2016-07
- Volume
- 1863
- Issue
- 7
- Pages
- 1490-1498
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2327684284
- Cited by
- 30
- References
- 0
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2023: 2 · 2022: 8 · 2021: 5 · 2020: 3 · 2018: 2 · 2017: 3
- FWCI
- 0.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- RISalud Institutional Health Repository of Andalucía (submittedVersion, other-oa)
- Funders
- Ministerio de Economía y Competitividad (BFU2012-37304/BFI)
- Consejo Superior de Investigaciones Científicas
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- SENP7, SUMO protease, SUMOylation, SUMO deconjugation, neuronal differentiation, neurogenesis, neural tube development, gene expression profiling, promoter activation, brain development
- MeSH terms
- Animals, Chick Embryo, Endopeptidases, Promoter Regions, Genetic, RNA, Messenger, Time Factors, Transfection, Tretinoin, Signal Transduction, Transcriptional Activation, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Developmental, Gene Expression Profiling, RNA Interference, Cell Line, Tumor, Mice, Neural Tube, Neurogenesis, Sumoylation, Neural Stem Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Sumo protease Senp7 is required for proper neuronal differentiation. https://app.cochat.ai/papers/10.1016/j.bbamcr.2016.03.028
- The paper
- Juarez-Vicente, F., Luna-Pelaez, N., & Garcia-Dominguez, M. (2016). The Sumo protease Senp7 is required for proper neuronal differentiation. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. https://doi.org/10.1016/j.bbamcr.2016.03.028