Evidence map›Paper›PMID 9482728›Full record

ArticleThe EMBO journal1998

A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3.

S Höning, I V Sandoval, K von Figura

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

90 citing papers in PubMed, 296 citations in OpenAlex.

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  11. AP-3-dependent targeting of flippase ATP8A1 to lamellar bodies suppresses activation of YAP in alveolar epithelial type 2 cells.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  15. The CLN3 gene and protein: What we know.Molecular genetics & genomic medicine · 2019
    Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

30 more citing papers are in PubMed but not listed here.

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.

S HöningInstitute for Biochemistry II, University of Göttingen, Gosslerstr. 12d, 37073 Göttingen, Germany.
I V Sandoval
K von Figura
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the various coats involved in vesicular transport, the clathrin associated coats that contain the adaptor complexes AP-1 and AP-2 are the most extensively characterized. The function of the recently described adaptor complex AP-3, which is similar to AP-1 and AP-2 in protein composition but does not associate with clathrin, is not known. By monitoring surface plasmon resonance we observed that AP-3 is able to interact with the tail of the lysosomal integral membrane protein LIMP-II and that this binding depends on a DEXXXLI sequence in the LIMP-II tail. Furthermore, AP-3 bound to the cytoplasmic tail of the melanosome-associated protein tyrosinase which contains a related EEXXXLL sequence. The tails of LIMP-II and tyrosinase either did not interact, or only interacted poorly, with AP-1 or AP-2. In contrast, the cytoplasmic tails of other membrane proteins containing di-leucine and/or tyrosine-based sorting signals did not bind AP-3, but AP-1 and/or AP-2. This points to a function of AP-3 in intracellular sorting to lysosomes and melanosomes of a subset of cargo proteins via di-leucine-based sorting motifs.

Indexed as

Monomeric Clathrin Assembly ProteinsAcid PhosphataseAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsAntigens, CDBiosensing TechniquesBrainCD36 AntigensCytoplasmCytosolLeucineLysosomal Membrane ProteinsLysosomesMelanocytesMembrane GlycoproteinsAcid PhosphataseAdaptor Proteins, Vesicular TransportAntigens, CDCD36 Antigensclathrin assembly protein AP180LeucineLysosomal Membrane ProteinsMembrane GlycoproteinsMonomeric Clathrin Assembly ProteinsMonophenol MonooxygenaseNerve Tissue ProteinsPeptidesPhosphoproteins

Identifiers

PMID9482728
PMCPMC1170479
OpenAlexW1973583404

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.