Evidence map›Paper›PMID 22582169›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Subpixel colocalization reveals amyloid precursor protein-dependent kinesin-1 and dynein association with axonal vesicles.

Lukasz Szpankowski, Sandra E Encalada, Lawrence S B Goldstein

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

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  9. A Role forFrontiers in cellular neuroscience · 2019
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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

3 authors at 1 institution in 2 countries.

Lukasz SzpankowskiBioinformatics and Systems Biology Graduate Program, Department of Bioengineering, University of California at San Diego, La Jolla, CA 92093, USA.
Sandra E Encalada
Lawrence S B Goldstein
Howard Hughes Medical Institute · US

Funding

U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
TRAINING IN THE NEUROPLASTICITY OF AGINGT32AG000216 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOO, EDWARD H. · 1992 to 2017
$8.4M
GRADUATE TRAINING PROGRAM IN BIONFORMATICST32GM008806 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAFNA, VINEET, REN, BING · 2001 to 2020
$6.2M
Impairment of axonal transport by Amyloid precursor protein and amyloid Beta-protR01AG032180 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GOLDSTEIN, LAWRENCE S. · 2007 to 2011
$1.6M
Howard Hughes Medical InstituteNIA NIH HHS AG000216NIA NIH HHS AG032180NIA NIH HHS R01 AG032180NIA NIH HHS T32 AG000216NIGMS NIH HHS T32 GM008806NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

Intracellular transport of vesicles and organelles along microtubules is powered by kinesin and cytoplasmic dynein molecular motors. Both motors can attach to the same cargo and thus must be coordinated to ensure proper distribution of intracellular materials. Although a number of hypotheses have been proposed to explain how these motors are coordinated, considerable uncertainty remains, in part because of the absence of methods for assessing motor subunit composition on individual vesicular cargos. We developed a robust quantitative immunofluorescence method based on subpixel colocalization to elucidate relative kinesin-1 and cytoplasmic dynein motor subunit composition of individual, endogenous amyloid precursor protein (APP) vesicles in mouse hippocampal cells. The resulting method and data allow us to test a key in vivo prediction of the hypothesis that APP can recruit kinesin-1 to APP vesicles in neuronal axons. We found that APP levels are well-correlated with the amount of the light chain of kinesin-1 (KLC1) and the heavy chain of cytoplasmic dynein (DHC1) on vesicles. In addition, genetic reduction of APP diminishes KLC1 and DHC1 levels on APP cargos. Finally, our data reveal that reduction of KLC1 leads to decreased levels of DHC1 on APP vesicles, suggesting that KLC1 is necessary for the association of DHC1 to these cargos, and help to explain previously reported retrograde transport defects generated when kinesin-1 is reduced.

Indexed as

Amyloid beta-Protein PrecursorAnimalsAnimals, NewbornAxonsCells, CulturedCytoplasmic DyneinsCytoplasmic VesiclesFemaleFluorescent Antibody TechniqueHippocampusKinesinsLuminescent ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutAmyloid beta-Protein PrecursorCytoplasmic DyneinsDync1h1 protein, mouseKinesinsKns2 protein, mouseLuminescent ProteinsMicrotubule-Associated Proteins

Identifiers

PMID22582169
PMCPMC3365224
OpenAlexW2016291326

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.