Evidence map›Paper›PMID 39369131›Full record

ArticleCellular and molecular life sciences : CMLS2024

AP-1B regulates interactions of epithelial cells and intraepithelial lymphocytes in the intestine.

Ryohtaroh Matsumoto, Kosuke Ogata, Daisuke Takahashi, Yusuke Kinashi, Takahiro Yamada, Ryo Morita, Keisuke Tanaka, Kouya Hattori, Mayumi Endo, Yumiko Fujimura and 5 more

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

15 authors.

Ryohtaroh MatsumotoDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Kosuke OgataDepartment of Molecular Systems BioAnalysis, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Daisuke TakahashiDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Yusuke KinashiDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Takahiro YamadaDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Ryo MoritaDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Keisuke TanakaDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Kouya HattoriDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Mayumi EndoDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Yumiko FujimuraDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan.
Nobuo SasakiLaboratory of Mucosal Ecosystem Design, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Japan.
Hiroshi OhnoLaboratory for Intestinal Ecosystem, RIKEN Center for Integrative Medical Science, Yokohama, Kanagawa, Japan.
Yasushi IshihamaDepartment of Molecular Systems BioAnalysis, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.
Shunsuke KimuraDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan. kimura-sn@keio.jp.ORCID http://orcid.org/0000-0001-9408-2884
Koji HaseDivision of Biochemistry, Graduate School of Pharmaceutical Science and Faculty of Pharmacy, Keio University, 1-5-30 Shiba Koen, Minato-ku, Tokyo, 105-8512, Japan. hase.a6@keio.jp.ORCID http://orcid.org/0000-0001-9550-2334

Funding

Asahi Glass Foundation FY2022Asahi Glass Foundation FY2023Core Research for Evolutional Science and Technology JPMJCR19H1Core Research for Evolutional Science and Technology JPMJCR19H3Core Research for Evolutional Science and Technology JPMJPR19H3Fuji Foundation for Protein Research FY2023Fuji Foundation for Protein Research FY2024Japan Agency for Medical Research and Development 22gm1310009h0003Japanese Society for Immunology (JP) Kibou ProjectsJapan Society for the Promotion of Science 19K07239Japan Society for the Promotion of Science 20H00509Japan Society for the Promotion of Science 20H05876Japan Society for the Promotion of Science 22K19445Japan Society for the Promotion of Science 23H02739Japan Society for the Promotion of Science 23H05482Keio University Doctorate Student Grant-in-Aid Program from Ushioda Memorial FundKeio University Program for the Advancement of Next Generation Research ProjectsMoonshot Research and Development Program JPMJMS2025Secom Science and Technology Foundation FY2022
6 · The paper itself

Abstract

Intraepithelial lymphocytes (IELs) reside in the epithelial layer and protect against foreign pathogens, maintaining the epithelial barrier function in the intestine. Interactions between IEL and epithelial cells are required for IELs to function effectively; however, the underlying molecular machinery remains to be elucidated. In this study, we found that intestinal epithelium-specific deficiency of the clathrin adaptor protein (AP)-1B, which regulates basolateral protein sorting, led to a massive reduction in IELs. Quantitative proteomics demonstrated that dozens of proteins, including known IEL-interacting proteins (E-cadherin, butyrophilin-like 2, and plexin B2), were decreased in the basolateral membrane of AP-1B-deficient epithelial cells. Among these proteins, CD166 interacted with CD6 on the surface of induced IEL. CD166 knockdown, using shRNA in intestinal organoid cultures, significantly inhibited IEL recruitment to the epithelial layer. These findings highlight the essential role of AP-1B-mediated basolateral sorting in IEL maintenance and survival within the epithelial layer. This study reveals a novel function of AP-1B in the intestinal immune system.

Indexed as

Adaptor Protein Complex 1Antigens, CDEpithelial CellsIntestinal MucosaIntraepithelial LymphocytesAdaptor Protein Complex mu SubunitsAnimalsCell Adhesion Molecules, NeuronalCell CommunicationIntestinesMiceMice, Inbred C57BLAdaptor Protein Complex 1Adaptor Protein Complex mu SubunitsAntigens, CDAp1m2 protein, mouseCell Adhesion Molecules, NeuronalAlcamInduced IELIodixanol density gradient ultracentrifugationNatural IELTMT-based quantitative proteome analysis

Identifiers

PMID39369131
PMCPMC11455912

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.