Evidence map›Paper›PMID 32052089›Full record

ReviewCellular and molecular life sciences : CMLS2020

Physiological functions of SPP/SPPL intramembrane proteases.

Torben Mentrup, Florencia Cabrera-Cabrera, Regina Fluhrer, Bernd Schröder

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Article
  2. Functional Characterization of a Signal Peptide Peptidase inInternational journal of molecular sciences · 2026
    Article
  3. Article
  4. Structural insights into human signal peptide peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Druggable genome screens identify SPP as an antiviral host target for multiple flaviviruses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Frontiers in immunology · 2024
    Article
  13. Article
  14. Common Markers and Small Molecule Inhibitors in Golgi Studies.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Membranes · 2022
    Article
  19. Article
  20. 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

4 authors.

Torben MentrupInstitute for Physiological Chemistry, Medizinisch-Theoretisches Zentrum MTZ, Technische Universität Dresden, Fiedlerstraße 42, 01307, Dresden, Germany.
Florencia Cabrera-CabreraInstitute for Physiological Chemistry, Medizinisch-Theoretisches Zentrum MTZ, Technische Universität Dresden, Fiedlerstraße 42, 01307, Dresden, Germany.
Regina FluhrerBiochemistry and Molecular Biology, Faculty of Medicine, University of Augsburg, Universitätsstraße 2, 86135, Augsburg, Germany.
Bernd SchröderInstitute for Physiological Chemistry, Medizinisch-Theoretisches Zentrum MTZ, Technische Universität Dresden, Fiedlerstraße 42, 01307, Dresden, Germany. bernd.schroeder@tu-dresden.de.ORCID http://orcid.org/0000-0003-0774-6270

Funding

Deutsche Forschungsgemeinschaft FL 635/2-2Deutsche Forschungsgemeinschaft FL 635/3-2Deutsche Forschungsgemeinschaft FOR2290Deutsche Forschungsgemeinschaft SCHR 1284/1-2Deutsche Forschungsgemeinschaft SCHR 1284/2-1Deutsche Forschungsgemeinschaft (DE) SFB877, B7
6 · The paper itself

Abstract

Intramembrane proteolysis describes the cleavage of substrate proteins within their hydrophobic transmembrane segments. Several families of intramembrane proteases have been identified including the aspartyl proteases Signal peptide peptidase (SPP) and its homologues, the SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3. As presenilin homologues, they employ a similar catalytic mechanism as the well-studied γ-secretase. However, SPP/SPPL proteases cleave transmembrane proteins with a type II topology. The characterisation of SPP/SPPL-deficient mouse models has highlighted a still growing spectrum of biological functions and also promoted the substrate discovery of these proteases. In this review, we will summarise the current hypotheses how phenotypes of these mouse models are linked to the molecular function of the enzymes. At the cellular level, SPP/SPPL-mediated cleavage events rather provide specific regulatory switches than unspecific bulk proteolysis. By this means, a plethora of different cell biological pathways is influenced including signal transduction, membrane trafficking and protein glycosylation.

Indexed as

Amyloid Precursor Protein SecretasesAnimalsAspartic Acid EndopeptidasesHumansMembrane ProteinsProtein TransportProteolysisSignal TransductionSubstrate SpecificityAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesMembrane Proteinssignal peptide peptidaseIntramembrane proteolysisMembrane traffickingProtein degradationSignal peptide peptidase-likeSignal transductionγ-secretase

Identifiers

PMID32052089
PMCPMC7366577

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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.