Evidence map›Paper›PMID 19295161›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009

The cleavage products of amyloid-beta precursor protein are sorted to distinct carrier vesicles that are independently transported within neurites.

Virgil Muresan, Nicholas H Varvel, Bruce T Lamb, Zoia Muresan

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 71 citations in OpenAlex.

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  16. Imaging the Intracellular Trafficking of APP with Photoactivatable GFP.Journal of visualized experiments : JoVE · 2015
    Article
  17. Review
  18. Article
  19. Differential release of β-amyloid from dendrite- versus axon-targeted APP.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
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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 2 institutions in 1 country.

Virgil MuresanDepartment of Pharmacology and Physiology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, Newark, New Jersey 07103, USA. muresavi@umdnj.edu
Nicholas H Varvel
Bruce T Lamb
Zoia Muresan
Case Western Reserve University · USRutgers New Jersey Medical School

Funding

Modifiers of Beta-Amyloid Metabolism and DepositionR01AG023012 · NIA · CLEVELAND CLINIC LERNER COM-CWRU · PI LAMB, BRUCE T · 2004 to 2013
$2.9M
Molecular Motors in Transport and Signaling by APPR01GM068596 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI MURESAN, VIRGIL · 2004 to 2009
$1.5M
NIA NIH HHS AG023012NIA NIH HHS R01 AG023012NIGMS NIH HHS GM068596NIGMS NIH HHS R01 GM068596
6 · The paper itself

Abstract

The amyloid-beta (Abeta) precursor protein (APP), a transmembrane protein that undergoes proteolytic cleavage into defined fragments, has been implicated in axonal transport. The proposed role of APP as a vesicle receptor for the microtubule motor kinesin-1 has relevance for the pathogenesis of Alzheimer's disease. Nevertheless, this function, which relies on the transport to the cell periphery of full-length APP rather than its cleavage fragments, remains controversial. Other proposed functions of APP, such as regulating transcription, neurogenesis, cell movement, or neurite growth also rely on APP's presence as a full-length protein at the cell surface, implying that APP cleavage occurs after its transport to the cell periphery. To test this hypothesis, we mapped the localization of various APP epitopes in neurons in culture and in the mouse brain. Surprisingly, epitopes from the N-terminal, C-terminal, and central (Abeta) domains of APP each showed a distinct distribution throughout the cell and rarely colocalized. Within neurites, these epitopes were localized to distinct transport vesicles that associated with different sets of microtubules and, occasionally, actin filaments. C-terminal APP fragments were preferentially transported into neurites as phosphorylated forms, entered the lamellipodium and filopodia of growth cones, and concentrated in regions of growth cone turning and advancement (unlike the N-terminal and Abeta fragments). We conclude that, under normal conditions, the proteolytic cleavage of APP primarily occurs before its sorting into axonal transport vesicles and the cleaved fragments segregate into separate vesicle populations that reach different destinations, and thus have different functions.

Indexed as

Amyloid beta-Protein PrecursorAnimalsAxonal TransportCells, CulturedHumansHydrolysisIntracellular FluidMiceMice, TransgenicNeuritesPeptide FragmentsProtein TransportSynaptic VesiclesAmyloid beta-Protein PrecursorPeptide Fragments

Identifiers

PMID19295161
PMCPMC2669751
OpenAlexW2155672037

What OpenQuestion holds

Textmetadata
LicenceTDM
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.