Evidence map›Paper›PMID 38890432›Full record

ArticleNature chemical biology2024

Quantitative control of subcellular protein localization with a photochromic dimerizer.

Takato Mashita, Toshiyuki Kowada, Hayashi Yamamoto, Satoshi Hamaguchi, Toshizo Sato, Toshitaka Matsui, Shin Mizukami

Abstract read
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In one paragraph

Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Proteins dance to the tune of light.Nature chemical biology · 2024
    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

7 authors.

Takato Mashita *Graduate School of Science, Tohoku University, Sendai, Japan.
Toshiyuki Kowada *Graduate School of Science, Tohoku University, Sendai, Japan.ORCID http://orcid.org/0000-0002-6623-6505
Hayashi YamamotoInstitute for Advanced Medical Sciences, Nippon Medical School, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0002-2831-1463
Satoshi HamaguchiGraduate School of Life Sciences, Tohoku University, Sendai, Japan.
Toshizo SatoGraduate School of Life Sciences, Tohoku University, Sendai, Japan.
Toshitaka MatsuiGraduate School of Science, Tohoku University, Sendai, Japan.ORCID http://orcid.org/0000-0003-3865-8468
Shin MizukamiGraduate School of Science, Tohoku University, Sendai, Japan. shin.mizukami@tohoku.ac.jp.ORCID http://orcid.org/0000-0002-2292-8606

Funding

Japan Agency for Medical Research and Development (AMED) 21gm1410006h0001MEXT | Japan Society for the Promotion of Science (JSPS) JP19H05284MEXT | Japan Society for the Promotion of Science (JSPS) JP20K05702MEXT | Japan Society for the Promotion of Science (JSPS) JP21H05252MEXT | Japan Society for the Promotion of Science (JSPS) JP21H05256MEXT | Japan Society for the Promotion of Science (JSPS) JP23H02077
6 · The paper itself

Abstract

Artificial control of intracellular protein dynamics with high precision provides deep insight into complicated biomolecular networks. Optogenetics and caged compound-based chemically induced dimerization (CID) systems are emerging as tools for spatiotemporally regulating intracellular protein dynamics. However, both technologies face several challenges for accurate control such as the duration of activation, deactivation rate and repetition cycles. Herein, we report a photochromic CID system that uses the photoisomerization of a ligand so that both association and dissociation are controlled by light, enabling quick, repetitive and quantitative regulation of the target protein localization upon illumination with violet and green light. We also demonstrate the usability of the photochromic CID system as a potential tool to finely manipulate intracellular protein dynamics during multicolor fluorescence imaging to study diverse cellular processes. We use this system to manipulate PTEN-induced kinase 1 (PINK1)-Parkin-mediated mitophagy, showing that PINK1 recruitment to the mitochondria can promote Parkin recruitment to proceed with mitophagy.

Indexed as

Protein KinasesUbiquitin-Protein LigasesDimerizationHeLa CellsHumansLightMitochondriaMitophagyPhotochemical ProcessesPTEN-Induced Putative Kinaseparkin proteinProtein KinasesPTEN-Induced Putative KinaseUbiquitin-Protein Ligases

Identifiers

What Socratic holds

Textmetadata
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.