Evidence map›Paper›PMID 25392300›Full record

ArticleMolecular biology of the cell2015

The catalytically inactive tyrosine phosphatase HD-PTP/PTPN23 is a novel regulator of SMN complex localization.

Alma Husedzinovic, Beate Neumann, Jürgen Reymann, Stefanie Draeger-Meurer, Ashwin Chari, Holger Erfle, Utz Fischer, Oliver J Gruss

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

22 citing papers in PubMed, 29 citations in OpenAlex.

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  12. Final Exon Frameshift BiallelicBrain sciences · 2021
    Article
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  16. Alteration of 28S rRNA 2'-Biology open · 2019
    Article
  17. Article
  18. Myopic (HD-PTP, PTPN23) selectively regulates synaptic neuropeptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Article
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

8 authors at 3 institutions in 1 country.

Alma HusedzinovicZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Universität Heidelberg, D-69120 Heidelberg, Germany.
Beate NeumannEuropean Molecular Biology Laboratory, Advanced Light Microscopy Facility Programme, D-69117 Heidelberg, Germany.
Jürgen ReymannViroQuant-CellNetworks RNAi Screening Facility, BioQuant Centre, Universität Heidelberg, D-69120 Heidelberg, Germany.
Stefanie Draeger-MeurerZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Universität Heidelberg, D-69120 Heidelberg, Germany.
Ashwin ChariTheodor Boveri Institute, Biocenter of the University of Würzburg, D-97074 Würzburg, Germany.
Holger ErfleViroQuant-CellNetworks RNAi Screening Facility, BioQuant Centre, Universität Heidelberg, D-69120 Heidelberg, Germany.
Utz FischerTheodor Boveri Institute, Biocenter of the University of Würzburg, D-97074 Würzburg, Germany.
Oliver J GrussZentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Alliance, Universität Heidelberg, D-69120 Heidelberg, Germany o.gruss@zmbh.uni-heidelberg.de.
Heidelberg University · DEUniversity of Würzburg · DEEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The survival motor neuron (SMN) complex fulfils essential functions in the assembly of snRNPs, which are key components in the splicing of pre-mRNAs. Little is known about the regulation of SMN complex activity by posttranslational modification despite its complicated phosphorylation pattern. Several phosphatases had been implicated in the regulation of SMN, including the nuclear phosphatases PPM1G and PP1γ. Here we systematically screened all human phosphatase gene products for a regulatory role in the SMN complex. We used the accumulation of SMN in Cajal bodies of intact proliferating cells, which actively assemble snRNPs, as a readout for unperturbed SMN complex function. Knockdown of 29 protein phosphatases interfered with SMN accumulation in Cajal bodies, suggesting impaired SMN complex function, among those the catalytically inactive, non-receptor-type tyrosine phosphatase PTPN23/HD-PTP. Knockdown of PTPN23 also led to changes in the phosphorylation pattern of SMN without affecting the assembly of the SMN complex. We further show interaction between SMN and PTPN23 and document that PTPN23, like SMN, shuttles between nucleus and cytoplasm. Our data provide the first comprehensive screen for SMN complex regulators and establish a novel regulatory function of PTPN23 in maintaining a highly phosphorylated state of SMN, which is important for its proper function in snRNP assembly.

Indexed as

BiocatalysisBlotting, WesternCell NucleusCoiled BodiesCytoplasmElectrophoresis, Gel, Two-DimensionalHeLa CellsHumansMicroscopy, ConfocalPhosphorylationProtein TransportProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorRibonucleoproteins, Small NuclearRNA InterferenceSMN Complex ProteinsProtein Tyrosine PhosphatasesProtein Tyrosine Phosphatases, Non-ReceptorPTPN23 protein, humanRibonucleoproteins, Small NuclearSMN Complex Proteins

Identifiers

PMID25392300
PMCPMC4294665
OpenAlexW1970485045

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.