bims-axbals Biomed News
on Axonal biology and ALS
Issue of 2026–02–01
nineteen papers selected by
TJ Krzystek



  1. Front Mol Neurosci. 2025 ;18 1667839
      Mutations in α-synuclein (α-syn) and LRRK2 cause familial Parkinson's disease (fPD), yet how these proteins functionally interact remain ambiguous. We previously showed that α-syn undergoes bi-directional transport within axons and influences mitochondrial health, while other studies suggested that LRRK2-G2019S disrupts the axonal transport of autophagic vesicles and mitochondria. Here we tested the hypothesis that α-syn and LRRK2 are functionally linked during axonal transport. Expression of human LRRK2-WT in Drosophila larval nerves caused modest CSP-containing axonal blockages whereas no defects were seen in LRRK2 loss of function mutants in contrast to other proteins directly involved in axonal transport. Surprisingly, fPD mutations in the GTPase (LRRK2-Y1699C) and WD40 (LRRK2-G2385R) domains suppressed axonal blocks compared to LRRK2-WT, while kinase-domain mutant G2019S enhanced them. Reducing kinesin-1 had no effect with LRRK2-WT, but increased axonal transport defects with LRRK2-G2385R suggesting a functional interaction between the LRRK2 WD40 domain and the anterograde transport machinery. Further, co-expression of α-syn with either the GTPase domain or WD40 domain LRRK2 fPD mutants significantly suppressed α-syn-mediated axonal transport defects, decreased stalled α-syn-vesicles, but did not alter α-syn-mediated neuronal cell death. Taken together, these results suggest that while LRRK2 itself may not play an independent role in axonal transport, its GTPase and WD40 domains likely associate functionally with α-syn during transport within axons.
    Keywords:  Drosophila; LRRK2; Parkinson’s disease; WD40 domain; axonal transport; α-syn
    DOI:  https://doi.org/10.3389/fnmol.2025.1667839
  2. Elife. 2026 Jan 26. pii: RP95576. [Epub ahead of print]13
      Neuronal aging and neurodegenerative diseases are accompanied by proteostasis collapse, while the cellular factors that trigger it have not been identified. Impaired mitochondrial transport in the axon is another feature of aging and neurodegenerative diseases. Using Drosophila, we found that genetic depletion of axonal mitochondria causes dysregulation of protein degradation. Axons with mitochondrial depletion showed abnormal protein accumulation and autophagic defects. Lowering neuronal ATP levels by blocking glycolysis did not reduce autophagy, suggesting that autophagic defects are associated with mitochondrial distribution. We found that eIF2β was increased by the depletion of axonal mitochondria via proteome analysis. Phosphorylation of eIF2α, another subunit of eIF2, was lowered, and global translation was suppressed. Neuronal overexpression of eIF2β phenocopied the autophagic defects and neuronal dysfunctions, and lowering eIF2β expression rescued those perturbations caused by depletion of axonal mitochondria. These results indicate the mitochondria-eIF2β axis maintains proteostasis in the axon, of which disruption may underlie the onset and progression of age-related neurodegenerative diseases.
    Keywords:  D. melanogaster; aging; autophagy; cell biology; mitochondria; neuronal proteostasis; protein aggregation; proteome
    DOI:  https://doi.org/10.7554/eLife.95576
  3. Cureus. 2025 Dec;17(12): e100305
      Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder involving the degeneration of upper motor neurons (UMNs) and lower motor neurons (LMNs). Although the cause of motor neuron (MN) degeneration in patients with ALS remains unknown, certain MN types (such as oculomotor neurons) and MNs within the Onuf (Onuf-Mannen) nucleus are preserved until the terminal stage. We previously generated mice with a selective knockout of adenosine deaminase acting on RNA 2 (ADAR2) in cholinergic neurons (ADAR2flox/flox /vesicular acetylcholine transporter (VAChT)-Cre.Fast; AR2). AR2 mice exhibit slow progressive loss of LMNs accompanied by TAR DNA-binding protein 43 (TDP-43) pathology against a background of insufficient editing at the GluA2 glutamine/arginine (Q/R) site due to ADAR2 deficiency. This model confirmed that insufficient editing at the GluA2 Q/R site, due to reduced ADAR2 activity, contributes to the pathogenesis of ALS. Furthermore, in AR2 mice, more frequent death of fast-fatigable motor neurons (FF MNs) was observed owing to differences in vulnerability under ADAR2-deficient conditions. Similar changes were observed during normal aging in the control mice. These findings suggest that investigating the characteristics of FF MNs may be useful for analyzing neuronal death in ALS. Recently, matrix metalloproteinase-9 (MMP-9), a marker of FF MNs, was reported to induce neurodegeneration. However, the distribution of MMP-9 in normal spinal MNs and its age-related changes remain unclear. Therefore, we investigated the MMP-9 expression patterns in normal mice at six and 12 months of age. In the present study, the number of MNs in the anterior horn (AH) decreased with age, as did the number of MMP-9-positive MNs. Furthermore, as aging has been shown to induce the abnormal localization of TDP-43 in MMP-9-positive MNs, these MNs were considered vulnerable to degeneration. These findings suggest that MMP-9 not only functions as a marker for FF MNs but may also act as a potentially useful marker for MNs prone to degeneration with TDP-43 pathology, or for early degeneration in both physiological aging and age-related diseases, including ALS. Future investigations of MMP-9 expression in patients with ALS and in ALS mouse models are considered useful for elucidating ALS pathogenesis.
    Keywords:  adenosine deaminase acting on rna 2 (adar2); amyotrophic lateral sclerosis (als); fast-fatigable motor neurons (ff mns); matrix metalloproteinase-9 (mmp-9); tar dna-binding protein 43 (tdp-43)
    DOI:  https://doi.org/10.7759/cureus.100305
  4. FEBS J. 2026 Jan 30.
      TDP-43 mislocalization and aggregation are common features of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). However, the mechanisms underlying the transition of nuclear TDP-43 to cytoplasmic aggregates, and their contribution to disease pathogenesis, remain poorly understood. To address this gap, we present a methodology to chemically control the assembly and disassembly of cytoplasmic TDP-43 condensates. By fusing TDP-43 to a phase separation-prone protein scaffold, we can induce the formation of cytoplasmic TDP-43 condensates or, conversely, promote nuclear localization upon addition of a disassembly molecule. TDP-43 accumulates into various assemblies, ranging from submicrometric puncta to larger aggregate-like structures that display hallmarks of proteinopathy in a concentration-dependent manner. Furthermore, oxidative stress drives the maturation of TDP-43 assemblies from puncta into aggregates through interactions with stress granule components. Finally, we show that cytoplasmic TDP-43 aggregates deplete nuclear endogenous TDP-43 and induce cytotoxicity. Collectively, these findings highlight the local cytoplasmic concentration of TDP-43 and stress exposure as key determinants in the onset of TDP-43 proteinopathy, providing a relevant model to study pathological TDP-43 aggregation.
    Keywords:  ALS; LLPS; TDP‐43; condensates; phase separation
    DOI:  https://doi.org/10.1111/febs.70429
  5. ACS Chem Neurosci. 2026 Jan 29.
      Progressive aggregation of TAR DNA-binding protein 43 (TDP-43) is a hallmark of numerous neurodegenerative diseases, including amyotrophic lateral sclerosis, frontotemporal dementia, Alzheimer's disease, and limbic predominant age-related TDP-43 encephalopathy (LATE). This highly conserved nuclear RNA/DNA-binding protein is involved in the regulation of RNA processing. The C-terminal domain (CTD) of TDP-43 plays a key role in protein solubility, cellular localization, and protein-protein interactions. CTD is rich in glycine, glutamine, and asparagine, which facilitate TDP-43 aggregation into amyloid oligomers and fibrils observed in the brain. In this study, we examine the role of lipid bilayers in the aggregation properties of the CTD of TDP-43. We found that lipid bilayers composed of anionic phosphatidylserine and cardiolipin accelerated TDP-43 aggregation. Although lipids did not alter the secondary structure, they altered the cytotoxicity that TDP-43 fibrils exerted to rat dopaminergic cells. Using molecular methods, we showed that TDP-43 fibrils damage cell endosomes. This causes aggregate leakage into the cytosol, where TDP-43 fibrils impair cell autophagy, simultaneously triggering a severe unfolded protein response in the endoplasmic reticulum. Our results indicate that TDP-43 aggregation may be linked to pathological changes in the lipid profiles of neurons.
    Keywords:  CTD TDP-43; cardiolipin; neurons; phosphatidylcholine; phosphatidylserine; qPCR
    DOI:  https://doi.org/10.1021/acschemneuro.5c00934
  6. Elife. 2026 Jan 27. pii: RP100340. [Epub ahead of print]13
      Corticospinal neurons (CSN) centrally degenerate in amyotrophic lateral sclerosis (ALS), along with spinal motor neurons, and loss of voluntary motor function in spinal cord injury (SCI) results from damage to CSN axons. For functional regeneration of specifically affected neuronal circuitry in vivo, or for optimally informative disease modeling and/or therapeutic screening in vitro, it is important to reproduce the type or subtype of neurons involved. No such appropriate in vitro models exist with which to investigate CSN selective vulnerability and degeneration in ALS, or to investigate routes to regeneration of CSN circuitry for ALS or SCI, critically limiting the relevance of much research. Here, we identify that the HMG-domain transcription factor Sox6 is expressed by a subset of NG2+ endogenous cortical progenitors in postnatal and adult cortex, and that Sox6 suppresses a latent neurogenic program by repressing proneural Neurog2 expression by progenitors. We FACS-purify these progenitors from postnatal mouse cortex and establish a culture system to investigate their potential for directed differentiation into CSN. We then employ a multi-component construct with complementary and differentiation-sharpening transcriptional controls (activating Neurog2, Fezf2, while antagonizing Olig2 with VP16:Olig2). We generate corticospinal-like neurons from SOX6+/NG2+ cortical progenitors and find that these neurons differentiate with remarkable fidelity compared with corticospinal neurons in vivo. They possess appropriate morphological, molecular, transcriptomic, and electrophysiological characteristics, without characteristics of the alternate intracortical or other neuronal subtypes. We identify that these critical specifics of differentiation are not reproduced by commonly employed Neurog2-driven differentiation. Neurons induced by Neurog2 instead exhibit aberrant multi-axon morphology and express molecular hallmarks of alternate cortical projection subtypes, often in mixed form. Together, this developmentally-based directed differentiation from cortical progenitors sets a precedent and foundation for in vitro mechanistic and therapeutic disease modeling, and toward regenerative neuronal repopulation and circuit repair.
    Keywords:  CSN; SOX6+/NG2+ progenitors; circuit repair; corticospinal neurons; directed differentiation; disease modeling; mouse; neuron regeneration; neuroscience; regenerative medicine; stem cells
    DOI:  https://doi.org/10.7554/eLife.100340
  7. J Cell Biol. 2026 Apr 06. pii: e202502035. [Epub ahead of print]225(4):
      Landscape expansion microscopy (land-ExM) is a light microscopy technique that visualizes both the lipid and protein ultrastructural context of cells. Achieving this level of detail requires both superresolution and a high signal-to-noise ratio. Although expansion microscopy (ExM) provides superresolution, obtaining high signal-to-noise images of both proteins and lipids remains challenging. land-ExM overcomes this limitation by using self-retention trifunctional anchors to significantly enhance protein and lipid signals in expanded samples. This improvement enables the accurate visualization of diverse membrane organelles and phase separations, as well as the 3D visualization of their contact sites. As a demonstration, we revealed triple-organellar contact sites among the stress granule, the nuclear tunnel, and the nucleolus. Overall, land-ExM offers a high-contrast superresolution platform that advances our understanding of how cells spatially coordinate interactions between membrane organelles and phase separations.
    DOI:  https://doi.org/10.1083/jcb.202502035
  8. Bio Protoc. 2026 Jan 20. 16(2): e5567
      Transfecting neurons remains technically challenging due to their sensitivity. Conventional methods, such as Lipofectamine 2000 or Lipofectamine RNAiMAX, often result in significant cytotoxicity, which limits their utility. Although lentiviral transfection offers high efficiency, it is hindered by high costs and complex procedures. This experiment employs a small interfering RNA (siRNA)-specific transfection reagent from the Kermey company. This reagent is a novel nanoparticle-based lipid material designed for the efficient delivery of oligonucleotides, including siRNA, into a wide range of cell types. Its efficacy in achieving high transfection efficiency in neurons, however, has not yet been established. After several days of in vitro neuronal culture, researchers can perform a simple transfection procedure using this reagent to achieve robust transfection efficiency. Notably, the protocol does not require medium replacement 6-8 h post-transfection, streamlining the workflow and minimizing cellular stress. Key features • Based on Kermey's siRNA-specific transfection reagent, we present a method for efficient in vitro transfection of siRNA into primary cultured mouse cortical neurons. • No observable adverse effects are detected in the transfected neurons during the entire experiment. • This method enables consistent and efficient knockdown of the target protein. • Phosphoglycerate dehydrogenase (PHGDH) siRNA and siNC (negative control) siRNA can be transfected into neuronal cells after 72 h of in vitro culture.
    Keywords:  Knockdown; Neuron; Neuronal culture; Transfection; siRNA
    DOI:  https://doi.org/10.21769/BioProtoc.5567
  9. Adv Sci (Weinh). 2026 Jan 27. e14783
      Alzheimer's disease (AD) is the leading cause of dementia worldwide. Nevertheless, its cellular and molecular mechanisms remain incompletely understood, partially due to inadequate disease models. To illuminate early changes in AD, we developed a cerebrocortical organoid (CO) model with improved methodology. Our COs produce excitatory and inhibitory neurons alongside glia, utilizing established isogenic wild-type and diseased human induced pluripotent stem cells (hiPSCs) carrying heterozygous familial AD mutations in PSEN1ΔE9/WT, PSEN1M146V/WT, or APPSwe/WT. In addition to amyloid-beta (Aβ) accumulation, the AD COs display time-progressive loss of monomeric Tau, and accumulation of aggregated high-molecular-weight (HMW) phospho(p)-Tau species (pT181 and pT217). They also exhibit neuronal hyperexcitability reminiscent of early electroencephalography (EEG) clinical findings and synapse loss in AD patient brains. Single-cell RNA-sequencing analyses of AD and WT control COs reveal significant divergent molecular abnormalities in excitatory vs. inhibitory neurons, with several pathways being upregulated in one while downregulated in the other, providing insight into AD phenotypes. Finally, we show that chronic dosing with autophagy activators, including a novel mTOR inhibitor-independent drug candidate, prevents pathologic Aβ and HMW p-Tau accumulation, normalizes hyperexcitability, and rescues synaptic loss in AD COs. Collectively, our results demonstrate this CO model as a useful platform for assessing early features of familial AD pathogenesis and for testing small-molecule candidate therapeutics.
    Keywords:  Alzheimer's disease; autophagy; cortical organoids; pTau oligomers; presenilin 1
    DOI:  https://doi.org/10.1002/advs.202514783
  10. Ageing Res Rev. 2026 Jan 23. pii: S1568-1637(26)00025-5. [Epub ahead of print]115 103033
      Lysosomes are responsible for clearing cellular waste and facilitating material recycling, thus playing a crucial role in maintaining cellular homeostasis and even in resisting the development of various diseases. Lysosomes are highly dynamic organelles. While typically exhibiting a vesicular morphology, lysosomes can remodel into tubular structures under specific conditions; this morphological plasticity underpins their functional complexity. Aging triggers significant lysosomal morphological remodeling and functional decline, contributing to the development of age-related diseases, notably neurodegenerative disorders. Although lysosomal function has been extensively studied in age-related diseases, the mechanisms driving aging-associated morphological alterations and their pathophysiological significance remain elusive. This review synthesizes current knowledge on the regulation of lysosomal morphology and its changes and functions during aging and in age-related diseases. We propose that altered lysosomal morphology represents not merely a hallmark of aging, but also a significant determinant of lysosomal and cellular functions during aging. Targeting lysosomal morphology holds promise as an emerging strategy for counteracting functional deterioration in aged lysosomes and mitigating associated disease pathogenesis.
    Keywords:  Aging; Lysosomes; Morphology; Tubulation; Vesicular enlargement
    DOI:  https://doi.org/10.1016/j.arr.2026.103033
  11. Int J Mol Sci. 2026 Jan 16. pii: 905. [Epub ahead of print]27(2):
      Neurodegenerative disorders are increasingly linked to a progressive decline in lysosomal function. Activating Transcription Factor EB (TFEB), a master regulator of lysosomal biogenesis and autophagy, has therefore emerged as a promising therapeutic strategy to enhance cellular clearance in these conditions. In this study, we identified KHS-101 as a novel TFEB activator through a high-throughput screen of blood-brain-barrier-permeable small molecules. We demonstrated that KHS-101 promotes TFEB nuclear translocation, enhances lysosomal biogenesis and proteolytic activity, and increases autophagic flux. Furthermore, KHS-101 significantly accelerates the degradation of pathogenic A53T mutant α-synuclein in a cellular model of Parkinson's disease, suggesting its potential to mitigate α-synuclein-mediated proteotoxicity and hold neuroprotective potential. Our findings identify KHS-101 as a potent TFEB activator and highlight the therapeutic potential of modulating the autophagy-lysosomal pathway for treating Parkinson's disease and related disorders.
    Keywords:  KHS-101; Parkinson’s disease; TFEB; autophagy–lysosome pathway; lysosome degradation; α-synuclein
    DOI:  https://doi.org/10.3390/ijms27020905
  12. J Cell Biol. 2026 Apr 06. pii: e202501023. [Epub ahead of print]225(4):
      Neuronal signaling requires large amounts of ATP, making neurons particularly sensitive to defects in energy homeostasis. Mitochondrial movement and energy production are therefore regulated to align local demands with mitochondrial output. Here, we report a pathway that arrests mitochondria in response to decreases in the ATP-to-AMP ratio, an indication that ATP consumption exceeds supply. In neurons and cell lines, low concentrations of the electron transport chain inhibitor antimycin A decrease the production of ATP and concomitantly arrest mitochondrial movement without triggering mitophagy. This arrest is accompanied by the accumulation of actin fibers adjacent to the mitochondria, which serve as an anchor that resists the associated motors. This arrest is mediated by activation of the energy-sensing kinase AMPK, which phosphorylates TRAK1. This mechanism likely helps maintain cellular energy homeostasis by anchoring energy-producing mitochondria in places where they are most needed.
    DOI:  https://doi.org/10.1083/jcb.202501023
  13. Adv Sci (Weinh). 2026 Jan 27. e17009
      Viral infection is one of the conditions that induce stress granule (SG) formation, a cellular defense mechanism that exerts antiviral effects. To counteract this host response, viruses have evolved a broad spectrum of strategies to inhibit SG formation. However, the molecular mechanisms underlying SG inhibition remain poorly understood. The nucleocapsid proteins play a critical role in virus replication and host interaction. Here, using Semliki Forest Virus (SFV) as a model, we uncover the function of the alphavirus nucleocapsid in SG inhibition. This inhibitory function depends on oligomerization mediated by an N-terminal α-helix and with a positively charged intrinsically disordered region (IDR). We show that SFV capsid directly competes with G3BP1 for RNA binding, thereby disrupting G3BP1-RNA liquid-liquid phase separation (LLPS) in vitro and SG assembly in cells. This mechanism is conserved across the alphavirus family but is not shared by the nucleocapsid of SARS-CoV-2 or other endemic viruses examined. Notably, expression of a peptide from SFV capsid is sufficient to inhibit SG formation induced by Amyotrophic Lateral Sclerosis (ALS)-associated mutations, suggesting potential therapeutic applications. Our findings reveal mechanistic insight into SG modulation by the viral capsid protein and provide a possible bioengineering tool for probing SG dynamics in health and disease.
    Keywords:  G3BP1; alphavirus capsid; biomolecular condensates; phase separation; stress granule
    DOI:  https://doi.org/10.1002/advs.202517009
  14. Amyotroph Lateral Scler Frontotemporal Degener. 2026 Jan 27. 1-10
      Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease marked by progressive degeneration of upper and lower motor neurons. Most forms of ALS associated with a suspected causal variant are inherited in an autosomal dominant manner. However, there is an important subset of autosomal recessive (AR) variants, often associated with early-onset or atypical clinical features. Advances in genetic sequencing have led to increased recognition of AR ALS. In this review, we focus on four key confirmed AR ALS-associated genes, which appear to be most common-ALS2, SPG11, OPTN, and the D90A variant of SOD1-reviewing their pathophysiology and unique clinical manifestations. We also highlight very rare AR mutations implicated in ALS, including SYNE1, ATP13A2, and FUS, and some associated with overlap syndromes or debated pathogenicity including SIGMAR1, ERLIN1, and ERLIN2. These genes are involved in an array of processes including axonal transport, endosomal trafficking, oxidative stress response, and autophagy, suggesting distinct mechanisms of motor neuron degeneration. Some forms of AR ALS more frequently present with juvenile onset and slower progression, but other genes are associated with broader phenotypic spectra. This includes overlap with hereditary spastic paraplegia (HSP) and hereditary ataxias. Understanding these AR forms of ALS may enhance diagnostic precision, improve prognostication, and may pave the way for targeted gene therapies. This review underscores the emerging significance of AR inheritance in ALS and calls for deeper investigation into its molecular and clinical dimensions.
    Keywords:  Amyotrophic lateral sclerosis; gene replacement; gene therapy; genetics; motor neuron disease; motor neurone disease
    DOI:  https://doi.org/10.1080/21678421.2026.2615110
  15. Front Cell Neurosci. 2025 ;19 1749755
      Neuronal communication depends on neuronal polarity and the integrity of axonal excitable domains, including the axon initial segment (AIS), nodes of Ranvier, and presynaptic terminals. In addition to the influence of neuronal input on their function and plasticity, recent evidence suggests that glial cells play a significant role in regulating these domains under both physiological and pathological conditions. In this context, this review focusses on the roles of astrocytes and microglia in the physiological modulation of the AIS and nodes of Ranvier and how these glial cells are involved in several pathological contexts, beyond its participation in the tripartite synapse. The AIS and nodes of Ranvier are not only essential for the initiation and propagation of neuronal signals but also serve as key sites of interaction with astrocytes and microglia. These interactions are crucial for maintaining neuronal excitability and overall neural circuit health. Disruptions in the interactions between glial cells and the AIS or nodes of Ranvier-whether caused by injury or disease-can profoundly affect central nervous system (CNS) function, emphasizing the importance of this dynamic relationship in both normal and pathological contexts. Recent studies have highlighted the roles of astrocytes and microglia in contacting the AIS and nodes of Ranvier, contributing to their structural plasticity, as well as in maintaining their homeostasis through the secretion of signaling factors and the regulation of ion concentrations in their microenvironment. However, the mechanisms underlying these regulatory processes remain largely unknown, and further research is required to elucidate how these interactions influence axonal physiology and contribute to axonal pathology.
    Keywords:  astrocytes; axon; axon initial segment; microglia; nodes of Ranvier
    DOI:  https://doi.org/10.3389/fncel.2025.1749755
  16. Acta Neuropathol. 2026 Jan 26. 151(1): 10
      Lewy body dementia (LBD), encompassing dementia with Lewy bodies and Parkinson's disease dementia, is neuropathologically defined by neuronal accumulation of α-synuclein encoded by the SNCA gene. Genetic risk factors strongly influence LBD susceptibility, including SNCA multiplication, particularly triplication, and the apolipoprotein E ε4 allele (APOE4), the strongest common genetic risk factor for LBD. While SNCA is predominantly expressed in neurons and APOE primarily in glial cells, how these genetic factors converge to impact neuronal vulnerability and regional pathology in the human brain remains poorly understood. Here, we applied spatial transcriptomics to postmortem temporal cortex tissue from LBD cases with SNCA triplication or different APOE genotypes, alongside age- and sex-matched controls, to map gene expression within intact cortical architecture. We identified layer 5 of the gray matter as a particularly vulnerable region, characterized by elevated SNCA expression, pronounced synaptic and metabolic dysregulation, and exacerbation of these alterations in APOE4 carriers. Reelin signaling emerged as a core Lewy body-associated pathway disrupted across cortical layers, validated in independent postmortem cohorts and human-induced pluripotent stem cell (iPSC)-derived cortical organoids. In contrast, white matter exhibited distinct molecular alterations, including disrupted myelination pathways, with APOE4 carriers showing increased myelin debris and glial responses compared with non-carriers. Cell-type deconvolution informed by single-nucleus RNA sequencing further revealed APOE4-associated impairments in neuronal vulnerability and intercellular communication. Together, these findings define spatially and cell-type-specific mechanisms through which SNCA dosage and APOE4 genotype impact LBD pathology, providing insight into regionally distinct disease processes and potential targets for genetically stratified therapeutic interventions.
    Keywords:   APOE ; SNCA ; Lewy body dementia; Reelin; Spatial transcriptomics
    DOI:  https://doi.org/10.1007/s00401-026-02981-z
  17. Neurobiol Dis. 2026 Jan 24. pii: S0969-9961(26)00025-2. [Epub ahead of print] 107281
      Dynamically coupled neural networks are fundamental to human cognition and behavior and are disrupted in neurodevelopmental disorders. The formation and dissolution of functional networks is thought to be driven by synchronized oscillatory bursts across large populations of neurons. The mechanisms driving the emergence of these rhythms, known as oscillogenesis, are not well understood, particularly in the human brain. Using multi-electrode arrays, we investigated oscillogenesis in human induced pluripotent stem cell 2D neural cultures at different developmental stages and under pharmacological challenges. We found that cultures exhibited nested oscillations that were reduced by GABAA receptor blockade and emerged earlier when the proportion of GABAergic neurons was increased. Pharmacological manipulations of voltage-gated potassium channels and cholinergic receptors modulated the pattern of nested oscillations. These results reveal the capacity of these 2D cultures to model oscillogenesis, and underscore the need for their continued refinement, paving the way for linking systems-level neural networks to human cognition and disease.
    Keywords:  Cholinergic system; Excitation/inhibition; Human induced pluripotent stem cell (hiPSC); Multi-electrode array; Oscillations; Potassium channels
    DOI:  https://doi.org/10.1016/j.nbd.2026.107281
  18. Cell. 2026 Jan 28. pii: S0092-8674(25)01487-4. [Epub ahead of print]
      Aggregation of the protein tau defines tauopathies, the most common age-related neurodegenerative diseases, which include Alzheimer's disease and frontotemporal dementia. Specific neuronal subtypes are selectively vulnerable to tau aggregation, dysfunction, and death. However, molecular mechanisms underlying cell-type-selective vulnerability are unknown. To systematically uncover the cellular factors controlling the accumulation of tau aggregates in human neurons, we conducted a genome-wide CRISPRi screen in induced pluripotent stem cell (iPSC)-derived neurons. The screen uncovered both known and unexpected pathways, including UFMylation and GPI anchor biosynthesis, which control tau oligomer levels. We discovered that the E3 ubiquitin ligase CRL5SOCS4 controls tau levels in human neurons, ubiquitinates tau, and is correlated with resilience to tauopathies in human disease. Disruption of mitochondrial function promotes proteasomal misprocessing of tau, generating disease-relevant tau proteolytic fragments and changing tau aggregation in vitro. These results systematically reveal principles of tau proteostasis in human neurons and suggest potential therapeutic targets for tauopathies.
    Keywords:  CRISPR screen; CUL5; SOCS4; neurodegeneration; protein aggregation; proteostasis; tau
    DOI:  https://doi.org/10.1016/j.cell.2025.12.038
  19. Cells. 2026 Jan 20. pii: 194. [Epub ahead of print]15(2):
      The endolysosomal system plays a pivotal role in cellular function. Before reaching lysosomes for degradation, the endocytosed cargoes are sorted at various stages of endosomal trafficking for recycling and/or rerouting. The proper execution of these processes depends on tightly regulated ion fluxes across endolysosomal membranes. Recent studies have demonstrated the importance of two-pore channels (TPCs), including TPC1 and TPC2, in endolysosomal trafficking. These channels are expressed in the membranes of distinct populations of endosomes and lysosomes, where they respond to nicotinic acid adenine dinucleotide phosphate (NAADP) and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2] to conduct Ca2+ and Na+ release from these acidic organelles. Here, we discuss the potential implications of Ca2+ and Na+ fluxes mediated by TPCs across endolysosomal membranes in the physiological and pathophysiological functions of these organellar channels.
    Keywords:  TPCN1; TPCN2; acidic organelle; calcium signaling; fission; fusion; osmosis; sodium efflux; tubulation; vesicle trafficking
    DOI:  https://doi.org/10.3390/cells15020194