Evidence map›Paper›PMID 17360967›Full record

ArticleMolecular biology of the cell2007

The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site.

Balraj Doray, Intaek Lee, Jane Knisely, Guojun Bu, Stuart Kornfeld

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

111 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Oncogenic Gα signaling requires AP-3-dependent recruitment to the endolysosomal compartment.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
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  5. Review
  6. Clathrin-mediated endocytosis of ERECTA family receptors is essential for proper stomatal development inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. FgAP1Journal of fungi (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

51 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

5 authors at 2 institutions in 1 country.

Balraj DorayDepartment of Internal Medicine and Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Intaek Lee
Jane Knisely
Guojun Bu
Stuart Kornfeld
Washington University in St. Louis · USPalmetto Hematology Oncology · 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 CA-08759NCI NIH HHS R01 CA008759NCI NIH HHS R37 CA008759
6 · The paper itself

Abstract

The clathrin adaptors AP-1 and AP-2 bind cargo proteins via two types of motifs: tyrosine-based Yxx phi and dileucine-based [DE]XXXL[LI]. Although it is well established that Yxx phi motifs bind to the mu subunits of AP-1 or AP-2, dileucine motifs have been reported to bind to either the mu or beta subunits of these adaptors as well as the gamma/sigma1 hemicomplex of AP-1. To clarify this controversy, the various subunits of AP-1 and AP-2 were expressed individually and in hemicomplex form in insect cells, and they were used in glutathione S-transferase pull-down assays to determine their binding properties. We report that the gamma/sigma1 or alpha/sigma2 hemicomplexes bound the dileucine-based motifs of several proteins quite strongly, whereas binding by the beta1/mu1 and beta2/mu2 hemicomplexes, and the individual beta or mu subunits, was extremely weak or undetectable. The gamma/sigma1 and alpha/sigma2 hemicomplexes displayed substantial differences in their preference for particular dileucine-based motifs. Most strikingly, an aspartate at position -4 compromised binding to the gamma/sigma1 hemicomplex, whereas minimally affecting binding to alpha/sigma2. There was an excellent correlation between binding to the alpha/sigma2 hemicomplex and in vivo internalization mediated by the dileucine-based sorting signals. These findings provide new insights into the trafficking mechanisms of D/EXXXL[LI]-mediated sorting signals.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex 2Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCHO CellsCricetinaeCricetulusDipeptidesGreen Fluorescent ProteinsHumansIn Vitro TechniquesMiceMultiprotein ComplexesProtein Sorting SignalsAdaptor Protein Complex 1Adaptor Protein Complex 2DipeptidesGreen Fluorescent ProteinsleucylleucineMultiprotein ComplexesProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID17360967
PMCPMC1855031
OpenAlexW2145410464

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.