Evidence map›Paper›PMID 35314681›Full record

ArticleNature communications2022

RUFY3 links Arl8b and JIP4-Dynein complex to regulate lysosome size and positioning.

Gaurav Kumar, Prateek Chawla, Neha Dhiman, Sanya Chadha, Sheetal Sharma, Kanupriya Sethi, Mahak Sharma, Amit Tuli

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 78 citations in OpenAlex.

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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 2 institutions in 1 country.

Gaurav KumarDivison of Cell Biology and Immunology, CSIR-Institute of Microbial Technology (IMTECH), Chandigarh, India.ORCID 0000-0001-9614-1032
Prateek ChawlaDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER), Mohali, Punjab, India.
Neha DhimanDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER), Mohali, Punjab, India.
Sanya ChadhaDivison of Cell Biology and Immunology, CSIR-Institute of Microbial Technology (IMTECH), Chandigarh, India.
Sheetal SharmaDivison of Cell Biology and Immunology, CSIR-Institute of Microbial Technology (IMTECH), Chandigarh, India.
Kanupriya SethiDivison of Cell Biology and Immunology, CSIR-Institute of Microbial Technology (IMTECH), Chandigarh, India.
Mahak SharmaDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER), Mohali, Punjab, India.ORCID 0000-0002-4117-4790
Amit TuliDivison of Cell Biology and Immunology, CSIR-Institute of Microbial Technology (IMTECH), Chandigarh, India. atuli@imtech.res.in.ORCID 0000-0001-5476-4127
Institute of Microbial Technology · INIndian Institute of Science Education and Research Mohali · IN

Funding

DBT-Wellcome Trust India Alliance IA/S/19/1/504270Wellcome Trust
6 · The paper itself

Abstract

The bidirectional movement of lysosomes on microtubule tracks regulates their whole-cell spatial arrangement. Arl8b, a small GTP-binding (G) protein, promotes lysosome anterograde trafficking mediated by kinesin-1. Herein, we report an Arl8b effector, RUFY3, which regulates the retrograde transport of lysosomes. We show that RUFY3 interacts with the JIP4-dynein-dynactin complex and facilitates Arl8b association with the retrograde motor complex. Accordingly, RUFY3 knockdown disrupts the positioning of Arl8b-positive endosomes and reduces Arl8b colocalization with Rab7-marked late endosomal compartments. Moreover, we find that RUFY3 regulates nutrient-dependent lysosome distribution, although autophagosome-lysosome fusion and autophagic cargo degradation are not impaired upon RUFY3 depletion. Interestingly, lysosome size is significantly reduced in RUFY3 depleted cells, which could be rescued by inhibition of the lysosome reformation regulatory factor PIKFYVE. These findings suggest a model in which the perinuclear cloud arrangement of lysosomes regulates both the positioning and size of these proteolytic compartments.

Indexed as

DyneinsLysosomesADP-Ribosylation FactorsCytoskeletal ProteinsEndosomesHeLa CellsHumansProtein TransportADP-Ribosylation FactorsARL8B protein, humanCytoskeletal ProteinsDyneinsRUFY3 protein, human

Identifiers

PMID35314681
PMCPMC8938454
OpenAlexW4220919142

What OpenQuestion holds

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LicenceCC BY
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.