Evidence map›Paper›PMID 21586796›Full record

ArticleJournal of lipid research2011

A novel conserved targeting motif found in ABCA transporters mediates trafficking to early post-Golgi compartments.

Michael F Beers, Arie Hawkins, Henry Shuman, Ming Zhao, Jennifer L Newitt, Jean Ann Maguire, Wenge Ding, Surafel Mulugeta

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Biomedicines · 2024
    Review
  3. Review
  4. 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
  5. Is ABCA1 a lipid transfer protein?Journal of lipid research · 2018
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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 2 countries.

Michael F BeersDepartment of Medicine, Pulmonary, Allergy, and Critical Care Division, University of Pennsylvania, Philadelphia, PA, USA.
Arie Hawkins
Henry Shuman
Ming Zhao
Jennifer L Newitt
Jean Ann Maguire
Wenge Ding
Surafel Mulugeta
Czech Academy of Sciences, Institute of Physiology · CZPulmonary and Allergy Associates · USUniversity of Pennsylvania · US

Funding

ABCA3: Biosynthesis, Trafficking, and Cellular Responses in Health and DiseaseR01HL090732 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI MULUGETA, SURAFEL · 2008 to 2012
$2.0M
Biosynthesis and Trafficking of Surfactant Protein C In Health and DiseaseR01HL119436 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI BEERS, MICHAEL FRANCIS · 2013 to 2017
$2.0M
Expression and function of ABCA3 in type 2 cellsR01HL087177 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI BEERS, MICHAEL FRANCIS · 2007 to 2010
$1.3M
NHLBI NIH HHS HL-087177NHLBI NIH HHS HL-090732NHLBI NIH HHS R01 HL087177NHLBI NIH HHS R01 HL090732NHLBI NIH HHS R01 HL119436
6 · The paper itself

Abstract

The ATP binding cassette, class A (ABCA) proteins are homologous polytopic transmembrane transporters that function as lipid pumps at distinct subcellular sites in a variety of cells. Located within the N terminus of these transporters, there exists a highly conserved xLxxKN motif of unknown function. To define its role, human ABCA3 was employed as a primary model representing ABCA transporters, while mouse ABCA1 was utilized to support major findings. Transfection studies showed colocalization of both transporters with surfactant protein C (SP-C), a marker peptide for successful protein targeting to lysosomal-like organelles. In contrast, alanine mutation of xLxxKN resulted in endoplasmic reticulum retention. As proof of principle, swapping xLxxKN for the known lysosomal targeting motif of SP-C resulted in post-Golgi targeting of the SP-C chimera. However, these products failed to reach their terminal processing compartments, suggesting that the xLxxKN motif only serves as a Golgi exit signal. We propose a model whereby an N-terminal signal sequence, xLxxKN, directs ABCA transporters to a post-Golgi vesicular sorting station where additional signals may be required for selective delivery of individual transporters to final subcellular destinations.

Indexed as

Amino Acid MotifsAnimalsATP Binding Cassette Transporter 1ATP-Binding Cassette TransportersCell Line, TumorEndoplasmic ReticulumGolgi ApparatusHumansLysosomesMiceMicroscopy, FluorescenceMolecular Sequence DataMutationPlasmidsProtein Sorting SignalsProtein Structure, TertiaryABCA1 protein, humanABCA3 protein, humanATP Binding Cassette Transporter 1ATP-Binding Cassette TransportersProtein Sorting SignalsPulmonary Surfactant-Associated Protein CRecombinant Fusion Proteins

Identifiers

PMID21586796
PMCPMC3139239
OpenAlexW2134323073

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.