Evidence map›Paper›PMID 17959829›Full record

ArticleMolecular biology of the cell2008

Mint3/X11gamma is an ADP-ribosylation factor-dependent adaptor that regulates the traffic of the Alzheimer's Precursor protein from the trans-Golgi network.

Punya Shrivastava-Ranjan, Victor Faundez, Guofu Fang, Howard Rees, James J Lah, Allan I Levey, Richard A Kahn

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Membrane trafficking in health and disease.Disease models & mechanisms · 2020
    Review
  5. Article
  6. Article
  7. Review
  8. TheThe Journal of biological chemistry · 2019
    Article
  9. Article
  10. Review
  11. Review
  12. Mint3 potentiates TLR3/4- and RIG-I-induced IFN-β expression and antiviral immune responses.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. X11/Mint genes control polarized localization of axonal membrane proteins in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    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

7 authors at 1 institution in 1 country.

Punya Shrivastava-RanjanDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322-3050, USA.
Victor Faundez
Guofu Fang
Howard Rees
James J Lah
Allan I Levey
Richard A Kahn
Emory University · US

Funding

The Emory Alzheimer's Disease CenterP50AG025688 · NIA · EMORY UNIVERSITY · PI LEVEY, ALLAN I · 2005 to 2019
$25.7M
Cellular Mechanisms of Neuronal Metal Transport and ToxicityR01GM077569 · NIGMS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2006 to 2016
$2.6M
Mechanisms of Endosome Trafficking in NeuronsR01NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2003 to 2012
$2.5M
Regulation of vesicular membrane traffic by ARF proteinsR01GM067226 · NIGMS · EMORY UNIVERSITY · PI KAHN, RICHARD A · 2003 to 2011
$2.3M
Mechanisms of Endosome Trafficking in NeuronsR56NS042599 · NINDS · EMORY UNIVERSITY · PI FAUNDEZ, VICTOR · 2008 to 2008
$339k
NIA NIH HHS AG-025688NIA NIH HHS P50 AG025688NIGMS NIH HHS GM-077569NIGMS NIH HHS GM-67226NIGMS NIH HHS R01 GM067226NIGMS NIH HHS R01 GM077569NINDS NIH HHS NS-42599NINDS NIH HHS R01 NS042599NINDS NIH HHS R56 NS042599
6 · The paper itself

Abstract

Beta-amyloid peptides (Abeta) are the major component of plaques in brains of Alzheimer's patients, and are they derived from the proteolytic processing of the beta-amyloid precursor protein (APP). The movement of APP between organelles is highly regulated, and it is tightly connected to its processing by secretases. We proposed previously that transport of APP within the cell is mediated in part through its sorting into Mint/X11-containing carriers. To test our hypothesis, we purified APP-containing vesicles from human neuroblastoma SH-SY5Y cells, and we showed that Mint2/3 are specifically enriched and that Mint3 and APP are present in the same vesicles. Increasing cellular APP levels increased the amounts of both APP and Mint3 in purified vesicles. Additional evidence supporting an obligate role for Mint3 in traffic of APP from the trans-Golgi network to the plasma membrane include the observations that depletion of Mint3 by small interference RNA (siRNA) or mutation of the Mint binding domain of APP changes the export route of APP from the basolateral to the endosomal/lysosomal sorting route. Finally, we show that increased expression of Mint3 decreased and siRNA-mediated knockdowns increased the secretion of the neurotoxic beta-amyloid peptide, Abeta(1-40). Together, our data implicate Mint3 activity as a critical determinant of post-Golgi APP traffic.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAlzheimer DiseaseAmyloid beta-PeptidesBrainCadherinsCarrier ProteinsCell Line, TumorEndosomesHumansMutationNerve Tissue ProteinsProtein Processing, Post-TranslationalProtein Structure, TertiaryProtein TransportAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAmyloid beta-PeptidesAPBA2 protein, humanAPBA3 protein, humanCadherinsCarrier ProteinsNerve Tissue ProteinsRNA, Small Interfering

Identifiers

PMID17959829
PMCPMC2174186
OpenAlexW2120481954

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.