ArticlebioRxiv : the preprint server for biology2025
NDR1/2 kinases regulate cell polarization and cell motility through Cdc42 GTPase and Pard3 signaling in mammalian cells.
Article in bioRxiv : the preprint server for biology, 2025. 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
5 authors.
Funding
Abstract
Controlling cell polarity and the directionality of cell motility is critical for effective cell migration during wound healing. NDR (nuclear dbf2-related) kinase pathways have roles in cell morphogenesis that are conserved from yeast to humans. Here, we reveal that knockdown of NDR1/2 kinases significantly alters cell size, shape, and the actin cytoskeleton, while reducing migration persistence and impairing cell polarization in wound healing assays. Mechanistically, we find that NDR1/2 kinases regulate the spatial and temporal dynamics of Cdc42 GTPase. Reduced NDR kinase levels increase Cdc42 GTPase activity and disrupt Pard3 subcellular location. NDR kinases phosphorylate Pard3 at Serine144, and overexpressing Pard3 can partially restore wound healing in NDR-depleted cells, an effect lost when Serine144 is mutated. Finally, we determine that NDR1 knockdown significantly impairs wound closure in human skin ex vivo wound healing assays, highlighting NDR kinase physiological importance. Collectively, this study demonstrates that NDR kinases modulate cell motility and polarization through the control of Pard3 and Cdc42 signaling in human fibroblasts.
Identifiers
What Socratic 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 Socratic graph.