Evidence map›Paper›PMID 30718729›Full record

ArticleScientific reports2019

CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo.

Katsuhiro Sawasato, Ryo Sato, Hanako Nishikawa, Naoki Iimura, Yuki Kamemoto, Kohki Fujikawa, Toshiyuki Yamaguchi, Yutetsu Kuruma, Yasushi Tamura, Toshiya Endo and 3 more

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Dark Side ofJournal of the American Chemical Society · 2026
    Article
  3. Article
  4. Article
  5. The versatile role of YidC in membrane protein biosynthesis and quality control.Biochimica et biophysica acta. Molecular cell research · 2025
    Review
  6. Article
  7. Review
  8. Pan-genome analysis ofFrontiers in microbiology · 2024
    Article
  9. Key contributions of a glycolipid to membrane protein integration.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

13 authors.

Katsuhiro SawasatoThe United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, 020-8550, Japan.
Ryo SatoThe United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, 020-8550, Japan.
Hanako NishikawaThe United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, 020-8550, Japan.
Naoki IimuraCryobiofrontier Research Center, Faculty of Agriculture, Iwate University, Morioka, Iwate, 020-8550, Japan.
Yuki KamemotoCryobiofrontier Research Center, Faculty of Agriculture, Iwate University, Morioka, Iwate, 020-8550, Japan.
Kohki FujikawaBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Kyoto, 619-0284, Japan.
Toshiyuki YamaguchiBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Kyoto, 619-0284, Japan.
Yutetsu KurumaEarth-Life Science Institute, Tokyo Institute of Technology, Meguro-ku, Tokyo, 152-8550, Japan.
Yasushi TamuraFaculty of Science, Yamagata University, Yamagata, Yamagata, 990-8560, Japan.ORCID 0000-0002-8462-0607
Toshiya EndoFaculty of Life Sciences, Kyoto Sangyo University, Kita-ku, Kyoto, 603-8555, Japan.
Takuya UedaDepartment of Computational Biology and Medical Sciences Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, 277-8562, Japan.ORCID 0000-0002-7760-8271
Keiko ShimamotoBioorganic Research Institute, Suntory Foundation for Life Sciences, Seika-cho, Kyoto, 619-0284, Japan.
Ken-Ichi NishiyamaThe United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate, 020-8550, Japan. nishiyam@iwate-u.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MPIase is a glycolipid that is involved in membrane protein integration. Despite evaluation of its functions in vitro, the lack of information on MPIase biosynthesis hampered verification of its involvement in vivo. In this study, we found that depletion of CdsA, a CDP-diacylglycerol synthase, caused not only a defect in phospholipid biosynthesis but also MPIase depletion with accumulation of the precursors of both membrane protein M13 coat protein and secretory protein OmpA. Yeast Tam41p, a mitochondrial CDP-diacylglycerol synthase, suppressed the defect in phospholipid biosynthesis, but restored neither MPIase biosynthesis, precursor processing, nor cell growth, indicating that MPIase is essential for membrane protein integration and therefore for cell growth. Consistently, we observed a severe defect in protein integration into MPIase-depleted membrane vesicles in vitro. Thus, the function of MPIase as a factor involved in protein integration was proven in vivo as well as in vitro. Moreover, Cds1p, a eukaryotic CdsA homologue, showed a potential for MPIase biosynthesis. From these results, we speculate the presence of a eukaryotic MPIase homologue.

Indexed as

Biosynthetic PathwaysAcetylglucosamineCapsid ProteinsEscherichia coli ProteinsGlycolipidsMembrane ProteinsMembrane Transport ProteinsModels, BiologicalNucleotidyltransferasesProtein TransportAcetylglucosamineCapsid Proteinscoat protein, Bacteriophage M13Escherichia coli ProteinsGlycolipidsMembrane ProteinsMembrane Transport ProteinsNucleotidyltransferasesphosphatidate cytidylyltransferaseYIDC protein, E coli

Identifiers

PMID30718729
PMCPMC6362211

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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.