ArticleCommunications biology2026
A histidine pseudokinase modulates polar growth and cell shape in Streptomyces venezuelae.
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.
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
2 authors.
Funding
Abstract
Polar growth and cell shape determination in mycelium-forming Streptomyces bacteria depends on the function of a polarly localised multiprotein complex that directs cell wall synthesis - the polarisome. This complex assembles around the essential cell polarity determinant DivIVA, alongside other largely unknown components. We report here the discovery of a conserved hybrid histidine kinase-like protein, PsmA, that interacts and co-localises with DivIVA at the hyphal tips. Deletion of psmA affects the shape and dynamics of the polarisome, leading to aberrant cell shape and hyphal hyperbranching. PsmA is a pseudokinase that lacks the critical histidine residue in its catalytic core. Our results suggest that PsmA tunes the dynamics and properties of the DivIVA-based polar organelle in streptomycetes in parallel to but not redundantly with Scy and FilP, two coiled-coil proteins known to influence polarisome properties. In summary, PsmA interacts with DivIVA and modulates the integrity of the growth zones at hyphal tips.
Indexed as
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.