Evidence map›Paper›PMID 18250197›Full record

ArticleThe Journal of cell biology2008

Binding of cargo sorting signals to AP-1 enhances its association with ADP ribosylation factor 1-GTP.

Intaek Lee, Balraj Doray, Jennifer Govero, Stuart Kornfeld

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

26 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Visualization of Protein Sorting at theFrontiers in cell and developmental biology · 2019
    Article
  8. Article
  9. Review
  10. Article
  11. Adaptor proteins involved in polarized sorting.The Journal of cell biology · 2014
    Review
  12. Article
  13. Cargo recognition in clathrin-mediated endocytosis.Cold Spring Harbor perspectives in biology · 2013
    Review
  14. The clathrin adaptor complexes as a paradigm for membrane-associated allostery.Protein science : a publication of the Protein Society · 2013
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Intaek LeeDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.
Balraj Doray
Jennifer Govero
Stuart Kornfeld
Washington University in St. Louis · US

Funding

STRUCTURE, BIOSYNTHESIS &FUNCTION OF GLYCOPROTEINSR37CA008759 · NCI · WASHINGTON UNIVERSITY · PI KORNFELD, STUART A · 1990 to 2018
$14.0M
Structure, Biosynthesis & Function of GlycoproteinsR01CA008759 · NCI · WASHINGTON UNIVERSITY · PI KORNFELD, STUART A · 1985 to 2023
$3.5M
NCI NIH HHS R01 CA-08759NCI NIH HHS R37 CA008759
6 · The paper itself

Abstract

The adaptor protein AP-1 is the major coat protein involved in the formation of clathrin-coated vesicles at the trans-Golgi network. The prevailing view is that AP-1 recruitment involves coincident binding to multiple low-affinity sites comprising adenosine diphosphate ribosylation factor 1 (Arf-1)-guanosine triphosphate (GTP), cargo sorting signals, and phosphoinositides. We now show that binding of cargo signal peptides to AP-1 induces a conformational change in its core domain that greatly enhances its interaction with Arf-1-GTP. In addition, we provide evidence for cross talk between the dileucine and tyrosine binding sites within the AP-1 core domain such that binding of a cargo signal to one site facilitates binding to the other site. The stable association of AP-1 with Arf-1-GTP, which is induced by cargo signals, would serve to provide sufficient time for adaptor polymerization and clathrin recruitment while ensuring the packaging of cargo molecules into the forming transport vesicles.

Indexed as

ADP-Ribosylation Factor 1AnimalsBinding SitesCattleClathrinClathrin-Coated VesiclesGuanosine TriphosphateHumansLeucinePolymersProtein BindingProtein ConformationProtein Structure, TertiaryProtein TransportSignal TransductionSubcellular FractionsADP-Ribosylation Factor 1ClathrinGuanosine TriphosphateLeucinePolymersTranscription Factor AP-1Tyrosine

Identifiers

PMID18250197
PMCPMC2234244
OpenAlexW2061517276

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.