Evidence map›Paper›PMID 41855176›Full record

ArticlePLoS genetics2026

A scaffold attachment factor PHM-2 regulates synaptic transmission through SLO-2 potassium channel in C. elegans.

Longgang Niu, Karthika Murugasen, Shannon Hanggodo, Sakia Ferdousy, Lishuang Zhu, Bojun Chen

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In one paragraph

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

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Longgang NiuDepartment of Neuroscience, University of Connecticut School of Medicine, Farmington, Connecticut United States of America.
Karthika MurugasenDepartment of Biological Sciences, University of North Texas, Denton, Texas, United States of America.
Shannon HanggodoFrank H. Netter MD School of Medicine, Quinnipiac University, North Haven, Connecticut, United States of America.ORCID https://orcid.org/0009-0005-4106-8014
Sakia FerdousyDepartment of Biological Sciences, University of North Texas, Denton, Texas, United States of America.
Lishuang ZhuDepartment of Biological Sciences, University of North Texas, Denton, Texas, United States of America.
Bojun ChenDepartment of Biological Sciences, University of North Texas, Denton, Texas, United States of America.ORCID https://orcid.org/0000-0002-1141-9101

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scaffold attachment factor B (SAFB) proteins are evolutionarily conserved DNA/RNA binding proteins that are involved in multiple processes of gene expression. These proteins are broadly expressed with particular high expression observed in the nervous system. However, their physiological roles in neurons are largely unclear. Here we show that PHM-2, the sole SAFB ortholog in C. elegans, regulates synaptic transmission at the neuromuscular junctions through an effect on SLO-2 potassium channel. We found that phm-2 mutants suppress a sluggish phenotype of worms expressing a hyperactive SLO-2 channel, greatly reduces SLO-2-mediated neuronal whole-cell currents, and enhances neuromuscular synaptic transmission. In addition, we found that PHM-2 genetically interacts with another DNA/RNA binding protein, HRPU-2/hnRNP U, to control SLO-2 expression through a posttranscriptional mechanism. These results reveal a novel function of a SAFB protein in regulating neuronal activity, and may help understand the physiological roles of SAFB proteins in the nervous system of other species.

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsDNA-Binding ProteinsSynaptic TransmissionAnimalsMembrane Transport ProteinsMutationNeuromuscular JunctionNeuronsRNA-Binding ProteinsCaenorhabditis elegans ProteinsDNA-Binding ProteinsMembrane Transport ProteinsRNA-Binding ProteinsSLO-2 protein, C elegans

Identifiers

PMID41855176
PMCPMC13016476

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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.