Evidence map›Paper›PMID 20215116›Full record

ArticleThe Journal of biological chemistry2010

Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).

Miguel Sánchez-Álvarez, Marta Montes, Noemí Sánchez-Hernández, Cristina Hernández-Munain, Carlos Suñé

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 31% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
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  4. The role of MeCP2 in learning and memory.Learning & memory (Cold Spring Harbor, N.Y.) · 2019
    Article
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  15. Article
  16. Roles for SUMO in pre-mRNA processing.Wiley interdisciplinary reviews. RNA
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Miguel Sánchez-ÁlvarezDepartments of Molecular Biology, Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain; Departments of Cell Biology and Immunology, Instituto de Parasitología y Biomedicina "López Neyra," Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain.
Marta MontesDepartments of Molecular Biology, Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain.
Noemí Sánchez-HernándezDepartments of Molecular Biology, Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain.
Cristina Hernández-MunainDepartments of Cell Biology and Immunology, Instituto de Parasitología y Biomedicina "López Neyra," Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain.
Carlos SuñéDepartments of Molecular Biology, Consejo Superior de Investigaciones Científicas, Armilla, 18100 Granada, Spain. Electronic address: csune@ipb.csic.es.
Consejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Modification of proteins by small ubiquitin-like modifier (SUMO) is emerging as an important control of transcription and RNA processing. The human factor TCERG1 (also known as CA150) participates in transcriptional elongation and alternative splicing of pre-mRNAs. Here, we report that SUMO family proteins modify TCERG1. Furthermore, TCERG1 binds to the E2 SUMO-conjugating enzyme Ubc9. Two lysines (Lys-503 and Lys-608) of TCERG1 are the major sumoylation sites. Sumoylation does not affect localization of TCERG1 to the splicing factor-rich nuclear speckles or the alternative splicing function of TCERG1. However, mutation of the SUMO acceptor lysine residues enhanced TCERG1 transcriptional activity, indicating that SUMO modification negatively regulates TCERG1 transcriptional activity. These results reveal a regulatory role for sumoylation in controlling the activity of a transcription factor that modulates RNA polymerase II elongation and mRNA alternative processing, which are discriminated differently by this post-translational modification.

Indexed as

Alternative SplicingTranscription, GeneticBase SequenceCell LineFluorescent Antibody TechniqueHumansMutationRNA InterferenceRNA, Small InterferingSmall Ubiquitin-Related Modifier ProteinsTrans-ActivatorsTranscriptional Elongation FactorsRNA, Small InterferingSmall Ubiquitin-Related Modifier ProteinsTCERG1 protein, humanTrans-ActivatorsTranscriptional Elongation Factors

Identifiers

PMID20215116
PMCPMC2865347
OpenAlexW2029439522

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.