Evidence map›Paper›PMID 35041644›Full record

ArticlePLoS biology2022

Occludin is a target of Src kinase and promotes lipid secretion by binding to BTN1a1 and XOR.

Yunzhe Lu, Tao Zhou, Chongshen Xu, Rui Wang, Deyi Feng, Jiyong Li, Xu Wang, Yu Kong, Guohong Hu, Xiangyin Kong and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-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

12 citing papers in PubMed, 18 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

11 authors at 3 institutions in 1 country.

Yunzhe LuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Tao ZhouSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Chongshen XuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID 0000-0003-3092-8769
Rui WangMolecular Imaging Core Facility, School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Deyi FengSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Jiyong LiSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Xu WangInstitute of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Shanghai, China.
Yu KongInstitute of Neuroscience, CAS Center for Excellence in Brain Science and Intelligence Technology, Chinese Academy of Sciences, Shanghai, China.
Guohong HuCAS Key Laboratory of Tissue Microenvironment and Tumor, Shanghai Institute of Nutrition and Health, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.
Xiangyin KongCAS Key Laboratory of Tissue Microenvironment and Tumor, Shanghai Institute of Nutrition and Health, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.
Pengfei LuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID 0000-0002-8306-9569
ShanghaiTech University · CNChinese Academy of Sciences · CNShanghai Institute of Nutrition and Health · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid droplets (LDs) have increasingly been recognized as an essential organelle for eukaryotes. Although the biochemistry of lipid synthesis and degradation is well characterized, the regulation of LD dynamics, including its formation, maintenance, and secretion, is poorly understood. Here, we report that mice lacking Occludin (Ocln) show defective lipid metabolism. We show that LDs were larger than normal along its biogenesis and secretion pathway in Ocln null mammary cells. This defect in LD size control did not result from abnormal lipid synthesis or degradation; rather, it was because of secretion failure during the lactation stage. We found that OCLN was located on the LD membrane and was bound to essential regulators of lipid secretion, including BTN1a1 and XOR, in a C-terminus-dependent manner. Finally, OCLN was a phosphorylation target of Src kinase, whose loss causes lactation failure. Together, we demonstrate that Ocln is a downstream target of Src kinase and promotes LD secretion by binding to BTN1a1 and XOR.

Indexed as

Lipid MetabolismAnimalsButyrophilinsFemaleLactationLipid DropletsMammary Glands, AnimalMiceMilkOccludinsrc-Family KinasesBtn1a1 protein, mouseButyrophilinsOccludinsrc-Family Kinases

Identifiers

PMID35041644
PMCPMC8797263
OpenAlexW4206301530

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.