Evidence map›Paper›PMID 39474119›Full record

ArticleChemical & biomedical imaging2024

Real-Time Tracking of Vesicles in Living Cells Reveals That Tau-Hyperphosphorylation Suppresses Unidirectional Transport by Motor Proteins.

Eunsang Lee, Donghee Kim, Yo Han Song, Kyujin Shin, Sanggeun Song, Minho Lee, Yeongchang Goh, Mi Hee Lim, Ji-Hyun Kim, Jaeyoung Sung and 1 more

Abstract read
In one paragraph

Article in Chemical & biomedical imaging, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

1 citing paper in PubMed.

  1. 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

11 authors.

Eunsang LeeDepartment of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.ORCID https://orcid.org/0000-0002-5774-8840
Donghee KimCreative Research Initiative Center for Chemical Dynamics in Living Cells, Chung-Ang University, Seoul 06974, Republic of Korea.
Yo Han SongDepartment of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.
Kyujin ShinMaterials Research & Engineering Center (MREC), R&D Division, Hyundai Motor Company, Uiwang 16082, Republic of Korea.ORCID https://orcid.org/0009-0009-6749-3595
Sanggeun SongCreative Research Initiative Center for Chemical Dynamics in Living Cells, Chung-Ang University, Seoul 06974, Republic of Korea.ORCID https://orcid.org/0000-0002-5827-3496
Minho LeeCreative Research Initiative Center for Chemical Dynamics in Living Cells, Chung-Ang University, Seoul 06974, Republic of Korea.
Yeongchang GohDepartment of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.
Mi Hee LimDepartment of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea.ORCID https://orcid.org/0000-0003-3377-4996
Ji-Hyun KimCreative Research Initiative Center for Chemical Dynamics in Living Cells, Chung-Ang University, Seoul 06974, Republic of Korea.
Jaeyoung SungCreative Research Initiative Center for Chemical Dynamics in Living Cells, Chung-Ang University, Seoul 06974, Republic of Korea.ORCID https://orcid.org/0000-0003-0712-296X
Kang Taek LeeDepartment of Chemistry, School of Physics and Chemistry, Gwangju Institute of Science and Technology (GIST), Gwangju 61005, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic vesicle transport by motor proteins along microtubules is a crucially active process underlying neuronal communication. It is known that microtubules are destabilized by tau-hyperphosphorylation, which causes tau proteins to detach from microtubules and form neurofibril tangles. However, how tau-phosphorylation affects the transport dynamics of motor proteins on the microtubule remains unknown. Here, we discover that the long-distance unidirectional motion of vesicle-motor protein multiplexes (VMPMs) in living cells is suppressed under tau-hyperphosphorylation, with the consequent loss of fast vesicle-transport along the microtubule. The VMPMs in hyperphosphorylated cells exhibit seemingly bidirectional random motion, with dynamic properties far different from those of VMPM motion in normal cells. We establish a parsimonious physicochemical model of VMPM's active motion that provides a unified, quantitative explanation and predictions for our experimental results. Our analysis reveals that, under hyperphosphorylation conditions, motor protein multiplexes have both static and dynamic motility fluctuations. The loss of fast vesicle-transport along the microtubule can be a mechanism of neurodegenerative disorders associated with tau-hyperphosphorylation.

Identifiers

PMID39474119
PMCPMC11504168

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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.