Evidence map›Paper›PMID 39424799›Full record

ArticleNature communications2024

De novo designed YK peptides forming reversible amyloid for synthetic protein condensates in mammalian cells.

Takayuki Miki, Masahiro Hashimoto, Hiroki Takahashi, Masatoshi Shimizu, Sae Nakayama, Tadaomi Furuta, Hisakazu Mihara

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026
    Article
  4. Article
  5. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
  6. 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

7 authors.

Takayuki Miki *School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan. miki@macro.t.u-tokyo.ac.jp.ORCID 0000-0002-1275-6556
Masahiro Hashimoto *School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.ORCID 0000-0003-4188-4853
Hiroki TakahashiSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Masatoshi ShimizuSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.ORCID 0009-0007-1784-1008
Sae NakayamaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.
Tadaomi FurutaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.ORCID 0000-0003-4568-9043
Hisakazu MiharaSchool of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama, Kanagawa, 226-8501, Japan.ORCID 0000-0003-3549-2036

Funding

MEXT | Japan Science and Technology Agency (JST) JPMJFR2251MEXT | Japan Science and Technology Agency (JST) JPMJFS2112MEXT | Japan Society for the Promotion of Science (JSPS) 21K14739MEXT | Japan Society for the Promotion of Science (JSPS) 23H05408MEXT | Japan Society for the Promotion of Science (JSPS) 23KJ0920
6 · The paper itself

Abstract

In mammalian cells, protein condensates underlie diverse cell functions. Intensive synthetic biological research has been devoted to fabricating liquid droplets using de novo peptides/proteins designed from scratch in test tubes or bacterial cells. However, the development of de novo sequences for synthetic droplets forming in eukaryotes is challenging. Here, we report YK peptides, comprising 9-15 residues of alternating repeats of tyrosine and lysine, which form reversible amyloid-like fibrils accompanied by binding with poly-anion species such as ATP. By genetically tagging the YK peptide, superfolder GFPs assemble into artificial liquid-like droplets in living cells. Rational design of the YK system allows fine-tuning of the fluidity and construction of multi-component droplets. The YK system not only facilitates intracellular reconstitution of simplified models for natural protein condensates, but it also provides a toolbox for the systematic creation of droplets with different dynamics and composition for in situ evaluation.

Indexed as

AmyloidPeptidesAdenosine TriphosphateAnimalsBiomolecular CondensatesGreen Fluorescent ProteinsHeLa CellsHumansAdenosine TriphosphateAmyloidGreen Fluorescent ProteinsPeptides

Identifiers

PMID39424799
PMCPMC11489810

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.