Evidence map›Paper›PMID 20080965›Full record

ArticleThe Journal of biological chemistry2010

Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain.

Brigitte Heller, Emmanuel Adu-Gyamfi, Whitney Smith-Kinnaman, Cliff Babbey, Mohsin Vora, Yi Xue, Robert Bittman, Robert V Stahelin, Clark D Wells

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

38 citing papers in PubMed, 66 citations in OpenAlex.

  1. Identification of AMOTL2 as an antiviral factor that enhances the human type I interferon response against Zika virus.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Alchemical Free Energy Calculations on Membrane-Associated Proteins.Journal of chemical theory and computation · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Cell Junctions in Hippo Signaling.Cold Spring Harbor perspectives in biology · 2018
    Review
  15. Article
  16. Article
  17. Article
  18. Loss of OCRL increases ciliary PI(4,5)PJournal of cell science · 2017
    Article
  19. Article
  20. Review
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

9 authors at 4 institutions in 1 country.

Brigitte HellerDepartment of Biochemistry and Molecular Biology, University of Indiana School ofMedicine, Indianapolis, Indiana 46202, USA.
Emmanuel Adu-Gyamfi
Whitney Smith-Kinnaman
Cliff Babbey
Mohsin Vora
Yi Xue
Robert Bittman
Robert V Stahelin
Clark D Wells
University of Notre Dame · USIndiana University – Purdue University Indianapolis · USIndiana University South Bend · USQueens College, CUNY · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polarity proteins promote the asymmetric organization of cells by orienting intracellular sorting mechanisms, such as protein trafficking and cytoskeletal assembly. The localization of individual polarity proteins in turn is often determined by association with factors that mediate contact with other cells or the substratum. This arrangement for the Par and Crb apical polarity complexes at the tight junction is disrupted by the adaptor protein Amot. Amot directly binds the scaffolding proteins Patj and Mupp1 and redistributes them and their binding partners from the plasma membrane to endosomes. However, the mechanism by which Amot is targeted to endosomes is unknown. Here, a novel lipid binding domain within Amot is shown to selectively bind with high affinity to membranes containing monophosphorylated phosphatidylinositols and cholesterol. With similar lipid specificity, Amot inserts into and tubulates membranes in vitro and enlarges perinuclear endosomal compartments in cells. Based on the similar distribution of Amot with cholesterol, Rab11, and Arf6, such membrane interactions are identified at juxtanuclear endocytic recycling compartments. Taken together, these findings indicate that Amot is targeted along with associated apical polarity proteins to the endocytic recycling compartment via this novel membrane binding domain.

Indexed as

ADP-Ribosylation Factor 6ADP-Ribosylation FactorsAngiomotinsAnimalsBinding SitesBiophysical PhenomenaCell CompartmentationCell LineCell PolarityCholesterolDogsEndocytosisEndosomesHumansIntercellular Signaling Peptides and ProteinsIntracellular MembranesADP-Ribosylation Factor 6ADP-Ribosylation FactorsAMOT protein, humanAngiomotinsARF6 protein, humanCholesterolIntercellular Signaling Peptides and ProteinsLiposomesMembrane LipidsMembrane ProteinsMicrofilament Proteinsrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsRecombinant Proteins

Identifiers

PMID20080965
PMCPMC2852970
OpenAlexW2053132501

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.