Evidence map›Paper›PMID 39085064›Full record

ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2024

Key contributions of a glycolipid to membrane protein integration.

Keiko Shimamoto, Kohki Fujikawa, Tsukiho Osawa, Shoko Mori, Kaoru Nomura, Ken-Ichi Nishiyama

Abstract readReview
In one paragraph

Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

6 authors.

Keiko ShimamotoBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Soraku-gun, Kyoto, Japan.ORCID http://orcid.org/0000-0003-1086-5756
Kohki FujikawaBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Soraku-gun, Kyoto, Japan.ORCID http://orcid.org/0000-0002-7929-3314
Tsukiho OsawaBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Soraku-gun, Kyoto, Japan.
Shoko MoriBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Soraku-gun, Kyoto, Japan.ORCID http://orcid.org/0000-0002-9309-8005
Kaoru NomuraBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Soraku-gun, Kyoto, Japan.ORCID http://orcid.org/0000-0002-0752-0290
Ken-Ichi NishiyamaDepartment of Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University, Morioka, Iwate, Japan.ORCID http://orcid.org/0000-0003-0478-4482

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of membrane protein integration involves molecular devices such as Sec-translocons or the insertase YidC. We have identified an integration-promoting factor in the inner membrane of Escherichia coli called membrane protein integrase (MPIase). Structural analysis revealed that, despite its enzyme-like name, MPIase is a glycolipid with a long glycan comprising N-acetyl amino sugars, a pyrophosphate linker, and a diacylglycerol (DAG) anchor. Additionally, we found that DAG, a minor membrane component, blocks spontaneous integration. In this review, we demonstrate how they contribute to Sec-independent membrane protein integration in bacteria using a comprehensive approach including synthetic chemistry and biophysical analyses. DAG blocks unfavorable spontaneous integrations by suppressing mobility in the membrane core, whereas MPIase compensates for this. Moreover, MPIase plays critical roles in capturing a substrate protein to prevent its aggregation, attracting it to the membrane surface, facilitating its insertion into the membrane, and delivering it to other factors. The combination of DAG and MPIase efficiently regulates the integration of membrane proteins.

Indexed as

Escherichia coliGlycolipidsMembrane ProteinsCell MembraneDiglyceridesEscherichia coli ProteinsDiglyceridesEscherichia coli ProteinsGlycolipidsMembrane Proteinsanti-aggregationglycan–protein interactionglycolipidmembrane mobilityN-acetyl amino sugarpyrophosphate

Identifiers

PMID39085064
PMCPMC11413397

What OpenQuestion holds

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Registered trials

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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.