Evidence map›Paper›PMID 28036022›Full record

ReviewInternational journal of molecular sciences2016

Subcellular Trafficking of Mammalian Lysosomal Proteins: An Extended View.

Catherine Staudt, Emeline Puissant, Marielle Boonen

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.0field-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

51 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Autophagy-lysosomal pathway in neurodegeneration.Molecular neurodegeneration advances · 2026
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Golgi defect as a major contributor to lysosomal dysfunction.Frontiers in cell and developmental biology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Enamel defects in Acp4Scientific reports · 2022
    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

3 authors at 1 institution in 1 country.

Catherine StaudtPhysiological Chemistry Laboratory-URPhyM, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium. catherine.staudt@unamur.be.
Emeline PuissantPhysiological Chemistry Laboratory-URPhyM, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium. emeline.puissant@unamur.be.
Marielle BoonenPhysiological Chemistry Laboratory-URPhyM, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium. marielle.boonen@unamur.be.
University of Namur · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysosomes clear macromolecules, maintain nutrient and cholesterol homeostasis, participate in tissue repair, and in many other cellular functions. To assume these tasks, lysosomes rely on their large arsenal of acid hydrolases, transmembrane proteins and membrane-associated proteins. It is therefore imperative that, post-synthesis, these proteins are specifically recognized as lysosomal components and are correctly sorted to this organelle through the endosomes. Lysosomal transmembrane proteins contain consensus motifs in their cytosolic regions (tyrosine- or dileucine-based) that serve as sorting signals to the endosomes, whereas most lysosomal acid hydrolases acquire mannose 6-phosphate (Man-6-P) moieties that mediate binding to two membrane receptors with endosomal sorting motifs in their cytosolic tails. These tyrosine- and dileucine-based motifs are tickets for boarding in clathrin-coated carriers that transport their cargo from the trans-Golgi network and plasma membrane to the endosomes. However, increasing evidence points to additional mechanisms participating in the biogenesis of lysosomes. In some cell types, for example, there are alternatives to the Man-6-P receptors for the transport of some acid hydrolases. In addition, several "non-consensus" sorting motifs have been identified, and atypical transport routes to endolysosomes have been brought to light. These "unconventional" or "less known" transport mechanisms are the focus of this review.

Indexed as

Protein Sorting SignalsAnimalsHumansHydrolasesLysosomesMammalsMembrane ProteinsProtein Processing, Post-TranslationalProtein TransportHydrolasesMembrane ProteinsProtein Sorting Signalsalternative receptorlysosomemannose 6-phosphatesorting motiftraffickingunconventional

Identifiers

PMID28036022
PMCPMC5297682
OpenAlexW2562247590

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.