Evidence map›Paper›PMID 40102465›Full record

ArticleNature communications2025

The stomatin-like protein StlP organizes membrane microdomains to govern polar growth in filamentous actinobacteria under hyperosmotic stress.

Xiaobo Zhong, Sarah S M Baur, Veronique M A Ongenae, Guillermo Guerrero Egido, Shraddha Shitut, Chao Du, Erik Vijgenboom, Gilles P van Wezel, Victor Carrion Bravo, Ariane Briegel and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

12 authors.

Xiaobo ZhongMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0001-9155-4380
Sarah S M BaurInstitute for General Microbiology, Christian-Albrechts-University of Kiel, Kiel, Germany.ORCID http://orcid.org/0009-0000-6795-9433
Veronique M A OngenaeMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.
Guillermo Guerrero EgidoMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.
Shraddha ShitutMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0002-2759-6508
Chao DuMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0003-3447-5293
Erik VijgenboomMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0002-5059-069X
Gilles P van WezelMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0003-0341-1561
Victor Carrion BravoDepartamento de Microbiología, Facultad de Ciencias, Campus Universitario de Teatinos s/n, Universidad de Málaga, 29010, Málaga, Spain.
Ariane BriegelMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands.ORCID http://orcid.org/0000-0003-3733-3725
Marc BramkampInstitute for General Microbiology, Christian-Albrechts-University of Kiel, Kiel, Germany.ORCID http://orcid.org/0000-0002-7704-3266
Dennis ClaessenMolecular Biotechnology, Institute of Biology, Leiden University, Leiden, The Netherlands. d.claessen@biology.leidenuniv.nl.ORCID http://orcid.org/0000-0002-0789-2633

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) BR2815/7-1Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research) VI.C.192.002
6 · The paper itself

Abstract

The cell wall represents an essential structure conserved among most bacteria, playing a crucial role in growth and development. While extensively studied model bacteria have provided insights into cell wall synthesis coordination, the mechanism governing polar growth in actinobacteria remains enigmatic. Here we identify the stomatin-like protein StlP as a pivotal factor for orchestrating polar growth in filamentous actinobacteria under hyperosmotic stress. StlP facilitates the establishment of a membrane microdomain with increased membrane fluidity, a process crucial for maintaining proper growth. The absence of StlP leads to branching of filaments, aberrant cell wall synthesis, thinning of the cell wall, and the extrusion of cell wall-deficient cells at hyphal tips. StlP interacts with key components of the apical glycan synthesis machinery, providing protection to filaments during apical growth. Introduction of StlP in actinobacteria lacking this protein enhances polar growth and resilience under hyperosmotic stress, accompanied by the formation of a membrane microdomain. Our findings imply that stomatin-like proteins, exemplified by StlP, confer a competitive advantage to actinobacteria encountering hyperosmotic stress. Given the widespread conservation of StlP in filamentous actinobacteria, our results propose that the mediation of polar growth through membrane microdomain formation is a conserved phenomenon in these bacteria.

Indexed as

ActinobacteriaBacterial ProteinsMembrane MicrodomainsMembrane ProteinsOsmotic PressureCell WallBacterial ProteinsMembrane Proteins

Identifiers

PMID40102465
PMCPMC11920096

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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.