Evidence map›Paper›PMID 41634455›Full record

ArticleCommunications biology2026

The endoplasmic reticulum displays high polarity with low protein aggregation in human cells.

Xinwei Hu, Junlin Chen, Ping Liu, Huaiyue Zhang, Yu Liu, Xin Zhang, Lei Wang

Abstract read
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Xinwei HuState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Junlin ChenZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Life Sciences, Research Center for Industries of the Future and Westlake University, Hangzhou, Zhejiang, China.
Ping LiuState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Huaiyue ZhangState Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center. CAS Key Laboratory of Separation Science for Analytical Chemistry. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.
Yu LiuState Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center. CAS Key Laboratory of Separation Science for Analytical Chemistry. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.ORCID http://orcid.org/0000-0002-0779-1488
Xin ZhangZhejiang Key Laboratory of Precise Synthesis of Functional Molecules, Department of Chemistry, School of Life Sciences, Research Center for Industries of the Future and Westlake University, Hangzhou, Zhejiang, China.ORCID http://orcid.org/0000-0001-6686-1645
Lei WangState Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. wanglei@ibp.ac.cn.ORCID http://orcid.org/0000-0002-5071-5800

Funding

Chinese Academy of Sciences (CAS) YSBR-075Ministry of Science and Technology of the People's Republic of China (Chinese Ministry of Science and Technology) 2021YFA1300800, 2022YFA1303000National Natural Science Foundation of China (National Science Foundation of China) 22477102, 22494700, 22494702National Natural Science Foundation of China (National Science Foundation of China) 32450227, 92254305, 32271204
6 · The paper itself

Abstract

Many physicochemical properties in the cellular milieu are important for cell function and survival. However, the polarity of different subcellular compartments and its role in protein condensate and aggregate formation within cells are less characterized. Here, we develop a method to compare the polarity in different subcellular compartments using the same polarity-sensitive solvatochromic fluorescent probe. Unexpectedly, the endoplasmic reticulum (ER) lumen displays a higher polarity and a more crowded environment than the cytosol in human cells. Polarity-decreasing and crowding-increasing hypertonic conditions induce condensate or aggregate formation of two intrinsically disordered proteins, with-no-lysine kinase 1 and Huntingtin gene (Htt) exon1 with an expanded polyQ stretch (Htt-polyQ), in the cytosol. However, targeting Htt-polyQ to the ER prevents its aggregation, suggesting that polarity but not crowding is more relevant to protein aggregation. Our results reveal the heterogeneity in subcellular polarity and crowding, and uncover previously unrecognized high-polarity in the ER lumen, which provides a unique environment for maintaining robust proteostasis.

Indexed as

Cell PolarityEndoplasmic ReticulumProtein AggregatesCytosolHumansHuntingtin ProteinHTT protein, humanHuntingtin ProteinProtein Aggregates

Identifiers

PMID41634455
PMCPMC12894662

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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.