Evidence map›Paper›PMID 30733280›Full record

ArticleEMBO reports2019

The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban.

Johannes Niemeyer, Torben Mentrup, Ronny Heidasch, Stephan A Müller, Uddipta Biswas, Rieke Meyer, Alkmini A Papadopoulou, Verena Dederer, Martina Haug-Kröper, Vivian Adamski and 10 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Genetic etiological spectrum of sperm morphological abnormalities.Journal of assisted reproduction and genetics · 2024
    Review
  5. Article
  6. Genome-Wide Identification of the SPP/SPPL Gene Family andInternational journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. 1700029I15Rik orchestrates the biosynthesis of acrosomal membrane proteins required for sperm-egg interaction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Genomic architecture and functional effects of potential human inversion supergenes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Physiological functions of SPP/SPPL intramembrane proteases.Cellular and molecular life sciences : CMLS · 2020
    Review
  17. Signaling Functions of Intramembrane Aspartyl-Proteases.Frontiers in cardiovascular medicine · 2020
    Review
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 7 institutions in 1 country.

Johannes NiemeyerBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany.
Torben MentrupBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany.
Ronny HeidaschZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Heidelberg, Germany.
Stephan A MüllerDZNE - German Center for Neurodegenerative Diseases, Munich, Germany.ORCID 0000-0003-3414-307X
Uddipta BiswasInstitute of Physiological Chemistry, Technische Universität Dresden, Dresden, Germany.
Rieke MeyerBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany.
Alkmini A PapadopoulouInstitute for Metabolic Biochemistry, Biomedical Center (BMC) München, Ludwig Maximilians University of Munich, Munich, Germany.
Verena DedererZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Heidelberg, Germany.
Martina Haug-KröperInstitute for Metabolic Biochemistry, Biomedical Center (BMC) München, Ludwig Maximilians University of Munich, Munich, Germany.
Vivian AdamskiBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany.
Renate Lüllmann-RauchInstitute of Anatomy, Christian-Albrechts-University of Kiel, Kiel, Germany.
Martin BergmannInstitute of Veterinary Anatomy, Justus Liebig University of Gießen, Gießen, Germany.
Artur MayerhoferCell Biology, Anatomy III, Biomedical Center (BMC) München, Ludwig Maximilians University of Munich, Munich, Germany.
Paul SaftigBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany.ORCID 0000-0003-2637-7052
Gunther WennemuthInstitute of Anatomy, University Hospital, Duisburg-Essen University, Essen, Germany.ORCID 0000-0003-3313-2475
Rolf JessbergerInstitute of Physiological Chemistry, Technische Universität Dresden, Dresden, Germany.
Regina FluhrerDZNE - German Center for Neurodegenerative Diseases, Munich, Germany.ORCID 0000-0002-9778-4643
Stefan F LichtenthalerDZNE - German Center for Neurodegenerative Diseases, Munich, Germany.ORCID 0000-0003-2211-2575
Marius K LembergZentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), DKFZ-ZMBH Allianz, Heidelberg, Germany.ORCID 0000-0002-0996-1268
Bernd SchröderBiochemical Institute, Christian-Albrechts-University of Kiel, Kiel, Germany bernd.schroeder@tu-dresden.de.ORCID 0000-0003-0774-6270
Christian-Albrechts-Universität zu Kiel · DEGerman Center for Neurodegenerative Diseases · DEHeidelberg University · DELudwig-Maximilians-Universität München · DETechnische Universität Dresden · DEJustus-Liebig-Universität Gießen · DEUniversity of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal peptide peptidase (SPP) and the four homologous SPP-like (SPPL) proteases constitute a family of intramembrane aspartyl proteases with selectivity for type II-oriented transmembrane segments. Here, we analyse the physiological function of the orphan protease SPPL2c, previously considered to represent a non-expressed pseudogene. We demonstrate proteolytic activity of SPPL2c towards selected tail-anchored proteins. Despite shared ER localisation, SPPL2c and SPP exhibit distinct, though partially overlapping substrate spectra and inhibitory profiles, and are organised in different high molecular weight complexes. Interestingly, SPPL2c is specifically expressed in murine and human testis where it is primarily localised in spermatids. In mice, SPPL2c deficiency leads to a partial loss of elongated spermatids and reduced motility of mature spermatozoa, but preserved fertility. However, matings of male and female

Indexed as

Amino Acid SequenceAnimalsAspartic Acid EndopeptidasesCalciumCalcium-Binding ProteinsCell MembraneEndoplasmic ReticulumFemaleGerm CellsHEK293 CellsHeLa CellsHomeostasisHumansMaleMembrane ProteinsMiceAspartic Acid EndopeptidasesCalciumCalcium-Binding ProteinsMembrane ProteinsPhospholambansignal peptide peptidaseSPPL2C protein, humanSppl2c protein, mouseintramembrane proteolysisphospholambansignal peptide peptidase‐like proteasesspermatogenesistail‐anchored proteins

Identifiers

PMID30733280
PMCPMC6399600
OpenAlexW2912646755

What OpenQuestion holds

Textmetadata
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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.