Evidence map›Paper›PMID 29712939›Full record

ArticleScientific reports2018

Essential Role of the a3 Isoform of V-ATPase in Secretory Lysosome Trafficking via Rab7 Recruitment.

Naomi Matsumoto, Mizuki Sekiya, Koujiro Tohyama, Eri Ishiyama-Matsuura, Ge-Hong Sun-Wada, Yoh Wada, Masamitsu Futai, Mayumi Nakanishi-Matsui

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-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

35 citing papers in PubMed, 47 citations in OpenAlex.

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  12. Lysosomal biogenesis and function in osteoclasts: a comprehensive review.Frontiers in cell and developmental biology · 2024
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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

8 authors at 3 institutions in 1 country.

Naomi MatsumotoDivision of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan.
Mizuki SekiyaDivision of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan.
Koujiro TohyamaThe Center for Electron Microscopy and Bio-Imaging Research, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan.
Eri Ishiyama-MatsuuraThe Center for Electron Microscopy and Bio-Imaging Research, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan.
Ge-Hong Sun-WadaDepartment of Biochemistry, Faculty of Pharmaceutical Sciences, Doshisha Women's College, Kyotanabe, Kyoto, 610-0395, Japan.
Yoh WadaDivision of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka, 567-0047, Japan.
Masamitsu FutaiDivision of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan.
Mayumi Nakanishi-MatsuiDivision of Biochemistry, School of Pharmacy, Iwate Medical University, Yahaba, Iwate, 028-3694, Japan. nakanim@iwate-med.ac.jp.
Iwate Medical University · JPDoshisha Women's College of Liberal Arts · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secretory lysosomes are required for the specialised functions of various types of differentiated cells. In osteoclasts, the lysosomal proton pump V-ATPase (vacuolar-type ATPase) is targeted to the plasma membrane via secretory lysosomes and subsequently acidifies the extracellular compartment, providing optimal conditions for bone resorption. However, little is known about the mechanism underlying this trafficking of secretory lysosomes. Here, we demonstrate that the lysosome-specific a3 isoform of the V-ATPase a subunit plays an indispensable role in secretory lysosome trafficking, together with Rab7, a small GTPase involved in organelle trafficking. In osteoclasts lacking a3, lysosomes were not transported to the cell periphery, and Rab7 was not localised to lysosomes but diffused throughout the cytoplasm. Expression of dominant-negative (GDP-bound form) Rab7 inhibited lysosome trafficking in wild-type cells. Furthermore, a3 directly interacted with the GDP-bound forms of Rab7 and Rab27A. These findings reveal a novel role for the proton pump V-ATPase in secretory lysosome trafficking and an unexpected mechanistic link with Rab GTPases.

Indexed as

AnimalsCytoplasmGene Expression Regulation, EnzymologicGuanosine DiphosphateHumansLysosomesMiceMice, KnockoutOrganellesProtein IsoformsProtein Transportrab27 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsVacuolar Proton-Translocating ATPasesGuanosine DiphosphateProtein IsoformsRab27a protein, mouserab27 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab7 GTP-binding proteins, mouserab GTP-Binding ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID29712939
PMCPMC5928161
OpenAlexW2805638868

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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.