ArticlebioRxiv : the preprint server for biology2026
Biomolecular condensation of cMLCK enables myosin motor phosphorylation in the heart.
Article in bioRxiv : the preprint server for 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.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The heart needs to adapt its output to the metabolic demands of the organism. Phosphorylation of the myosin motors by cardiac myosin light chain kinase (cMLCK) increases heart muscle contractile function, yet its regulation and mechanism of action have remained unclear. Here, we show that cMLCK undergoes liquid-liquid phase separation and forms biomolecular condensates associated with the sarcoplasmic reticulum of cardiac muscle cells. Condensates selectively enrich enzymatic cofactors and substrates, which increases the catalytic activity of cMLCK. Our study reveals that cMLCK is fine-tuned to work in the molecular environment of condensates, enabling physiologically relevant levels of cardiac myosin motor phosphorylation. These findings establish a condensate-based mechanism for the spatial and temporal regulation of cardiac thick filament contractile function.
Identifiers
What OpenQuestion holds
Registered trials
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.