bims-axbals Biomed News
on Axonal biology and ALS
Issue of 2026–03–29
twenty-two papers selected by
TJ Krzystek



  1. Biomolecules. 2026 Mar 05. pii: 393. [Epub ahead of print]16(3):
      Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease for which there is currently no cure. Dominant mutations in the TARDBP gene are causative of ALS. In particular, the p. G376D substitution in TDP-43 causes familial ALS and it is associated with TDP-43 mislocalization in the cytosol, increased presence of cytoplasmic aggregates, and lysosomal and mitochondrial dysfunction. We previously designed a small interfering RNA (siRNA) that specifically targets and silences the mutant allele and we demonstrated that, in patient-derived fibroblasts, it can reduce TDP-43 aggregation, decrease oxidative stress, and improve cell viability. Here, we investigated the ability of this siRNA to revert some ALS-associated pathological phenotypes in motor neurons derived from induced pluripotent stem cells (iPSCs), as motor neurons are the primary cells affected in ALS. siRNA treatment reduced TDP-43 mislocalization, enhanced lysosomal function and cell viability, and decreased oxidative stress. These findings indicate that this allele-specific siRNA effectively reverses key ALS-related cellular deficits in motor neurons, representing a promising candidate for targeted therapy in patients carrying the TDP-43 G376D mutation.
    Keywords:  ALS; RNA interference; TARDBP; motor neuron
    DOI:  https://doi.org/10.3390/biom16030393
  2. Front Neurosci. 2026 ;20 1802313
      Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by progressive loss of upper and lower motor neurons. Despite marked genetic and pathological heterogeneity, a unifying pathogenic framework remains lacking. We propose that axonal transport impairment represents an early and convergent but genotype-modulated upstream vulnerability in ALS, contributing to distal synaptic failure, bioenergetic stress, protein aggregation, neuroinflammation, and neuronal death. Across many ALS models, including SOD1, TARDBP (TDP-43), FUS, and C9orf72, transport deficits are frequently detectable in presymptomatic stages, often preceding overt motor neuron loss or clinical manifestation, although temporal ordering varies by molecular subtype. Human data from induced pluripotent stem cell-derived motor neurons and neuroimaging in mutation carriers further support early transport dysfunction in both familial and sporadic ALS. We synthesize genetic, cellular, and systems-level evidence demonstrating that diverse ALS-associated mutations converge on intracellular trafficking machinery through distinct but interacting mechanisms, disrupting long-range cargo delivery and clearance in motor neurons. This framework provides a mechanistic basis for selective motor neuron vulnerability, the dying-back pattern of neuromuscular junction degeneration, and the emergence of downstream pathological hallmarks including mitochondrial dysfunction, excitotoxicity, aggregation, and inflammation. This model generates testable predictions regarding presymptomatic transport biomarkers and the timing of therapeutic intervention. We discuss implications for biomarker development and therapeutic strategy, proposing restoration of axonal transport as a central component of rational multimodal disease modification in ALS.
    Keywords:  amyotrophic lateral sclerosis; axonal transport; biomarkers; neurodegeneration; neuromuscular junction
    DOI:  https://doi.org/10.3389/fnins.2026.1802313
  3. Acta Neuropathol. 2026 Mar 26. pii: 32. [Epub ahead of print]151(1):
      Selective vulnerability of motor neurons is a defining feature of amyotrophic lateral sclerosis (ALS) and provides a valuable framework for uncovering mechanisms that distinguish resilient from vulnerable neuronal populations. We investigated whether dysregulation of neuroprotective microRNAs (miRNAs), miR-9-5p and miR-124-3p, contributes to the differential susceptibility of motor neuron subtypes. We focused on cervical spinal motor neurons (SMNs), which undergo drastic degeneration in ALS, and oculomotor neurons (OMNs), which remain functionally intact and rarely degenerate, allowing preservation of eye movement in ALS patients. Using a modified multiplexed fluorescent in situ hybridization protocol combined with immunofluorescence, we quantified the expression of miR-9-5p and miR-124-3p in cervical SMNs and OMNs from ALS and control cases. We observed significant downregulation of both miRNAs in ALS SMNs, while their expression was maintained in ALS OMNs. Stratification of ALS SMNs by TDP-43 pathological status revealed similarly reduced miRNA expression in neurons with and without cytoplasmic inclusions, suggesting that miRNA downregulation occurs independently of visible TDP-43 pathology. We assessed the localization of the Dicer cofactor TRBP and found that it colocalized with TDP-43 inclusions in ALS SMNs, suggesting that TRBP sequestration could prevent proper miRNA processing. However, TRBP remained normally localized in neurons without cytoplasmic inclusions, indicating that sequestration cannot fully account for miRNA reduction across all ALS motor neurons. These findings support a model in which early or subtle disruptions, preceding visible pathology, may also contribute to miRNA downregulation in ALS. By identifying preserved miRNA networks as correlates of oculomotor neuron resilience in ALS, this work also exposes new therapeutic targets potentially capable of reinstating miRNA expression and reprogramming vulnerable SMNs.
    Keywords:  Amyotrophic lateral sclerosis; Fluorescent in situ hybridization; Selective motor neuron vulnerability; TDP-43; miR-124-3p; miR-9-5p
    DOI:  https://doi.org/10.1007/s00401-026-03005-6
  4. PLoS Biol. 2026 Mar;24(3): e3003662
      TDP-43 pathology is a hallmark of fatal neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TDP-43-encephalopathy (LATE). In affected patients, cytoplasmic TDP-43 aggregates are accompanied by disruption of its normal nuclear localization and function. Because TDP-43 is an RNA binding protein that controls transcript processing, including repression of cryptic exon splicing, its loss leads to dysregulation of gene expression. Despite its central significance in disease, the connection between TDP-43 aggregation and dysfunction remains poorly understood, and models to study the underlying mechanisms are limited. Here, we characterize a robust and quantitative cell-based reporter that captures both aggregation and the resulting loss of function. Using this human biosensor cell line, we show that aggregation initiated by prion-like seeding drives progressive depletion of nuclear TDP-43 and induces signature features of diminished TDP-43 activity, such as increased DNA damage and activation of cryptic exon splicing. We find that aggregate seeding also induces cryptic exon splicing in human neurons implying that this pathological link extends to disease-relevant models. The seeding model provides a platform for dissecting mechanisms that underlie TDP-43 pathology and for identifying factors that modulate the aggregation-to-dysfunction transition. Our data shows that aggregate seeding impacts TDP-43 autoregulation, initiating a toxic feed-forward mechanism that disrupts TDP-43 homeostasis. Furthermore, reducing ataxin-2 levels decreases aggregation and restores TDP-43 activity. Together, these findings reveal a molecularly guided strategy to directly impact TDP-43 activity by decreasing its misfolding and aggregation, highlighting approaches to prevent TDP-43 dysfunction and mitigate toxicity under pathological conditions.
    DOI:  https://doi.org/10.1371/journal.pbio.3003662
  5. Transl Neurodegener. 2026 Mar 24. pii: 13. [Epub ahead of print]15(1):
      Axons are unique structural and functional features of nerve cells, which play a critical role in regulating neuronal homeostasis. Dysfunction and degeneration of axons (axonopathy) has been established as an early and prominent contributing mechanism to the pathogenesis of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, Huntington's disease, and amyotrophic lateral sclerosis. In this review, we briefly summarize the structure and function of axons, and highlight recent advances in the understanding of the role of axons in health and disease. We argue that axons are a potential target for developing novel therapies for neurodegenerative diseases.
    Keywords:  Alzheimer’s disease; Amyotrophic lateral sclerosis; Autophagy; Axon; Axonal transport; Huntington’s disease; Mitochondria; Neurodegeneration; Neurotrophic factors; Parkinson’s disease
    DOI:  https://doi.org/10.1186/s40035-026-00543-7
  6. bioRxiv. 2026 Mar 16. pii: 2026.03.14.711828. [Epub ahead of print]
      Quantitative evaluation of protein turnover in human neurons is crucial for understanding neuron homeostasis and guiding drug development for neurological diseases. However, measuring protein turnover in postmitotic neurons remains challenging due to the high dynamic range of protein half-lives and limited proteome coverage in SILAC (Stable Isotope Labeling by Amino acids in Cell culture) experiments. Despite broad applications of dynamic SILAC proteomics to measure protein turnover in rodent tissues and primary neurons, few studies have measured protein half-lives in human neurons with limited proteome coverage. Here, we established a comprehensive platform to quantify protein half-lives in human induced pluripotent stem cell (iPSC)-derived neurons. By integrating optimized dynamic SILAC labeling in human neuron cultures, extensive peptide fractionation, optimized data-dependent and data-independent LC-MS/MS acquisition methods, and a streamlined computational pipeline, we achieved deep and accurate measurement of 10,792 protein half-lives from 162,854 unique peptides. We then compared the protein turnover and abundances in iPSC-derived glutamatergic cortical neurons and spinal motor neurons, revealing globally conserved proteome dynamics alongside subtype-specific differences consistent with specialized neuronal functions. To enable broad community access, we created NeuronProfile ( www.neuronprofile.com ), an interactive web platform for exploring protein turnover, abundance, and subcellular location in human neurons. Together, this work provides a comprehensive analytical platform to assess human neuronal proteostasis and a foundational resource for neurological disease research and therapeutic development.
    DOI:  https://doi.org/10.64898/2026.03.14.711828
  7. JCI Insight. 2026 Mar 26. pii: e197941. [Epub ahead of print]
      Spinal muscular atrophy (SMA) is a devastating neuromuscular disorder caused by mutations in the survival motor neuron 1 (SMN1) gene leading to decreased SMN protein levels and motor neuron dysfunction. SMN-restoring therapies offer clinical benefit, but the downstream molecular consequences of SMN reduction remain incompletely understood. SMN deficiency resulted in downregulation of kinesin heavy chain isoform 5A (KIF5A) in human neurons and in a mouse model of SMA. SMN associated with KIF5A mRNA and contributed to its stability. Reduced SMN levels impaired axon regeneration, which was rescued by KIF5A overexpression. Because KIF5A has also been connected to ALS, these findings provide evidence of a molecular link between SMA and ALS pathophysiology, highlighting KIF5A as an SMN regulated factor. Our findings suggest SMN-independent interventions targeting KIF5A could represent a complementary therapeutic approach for SMA and other motor neuron diseases.
    Keywords:  Genetics; Neuromuscular disease; Neuroscience
    DOI:  https://doi.org/10.1172/jci.insight.197941
  8. Curr Neuropharmacol. 2026 Mar 16.
      Neurodegenerative disorders (NDs), including Alzheimer's disease (AD), Parkinson's disease (PD), and amyotrophic lateral sclerosis (ALS), are characterized by the accumulation of misfolded proteins and impaired cellular clearance mechanisms. Autophagy, a critical lysosomedependent degradative pathway, plays a vital role in maintaining proteostasis and neuronal health. Dysregulation of autophagy has been implicated in the pathogenesis of multiple NDs, making it a promising therapeutic target. This review comprehensively examines the molecular mechanisms of autophagy and its dysfunction across major NDs. Furthermore, it highlights the potential of bioactive compounds such as flavonoids, alkaloids, polyphenols, and terpenoids to modulate autophagic flux, thereby promoting the clearance of toxic protein aggregates like amyloid-β, tau, and α- synuclein. Emerging strategies, including nanotechnology-based delivery systems, are also discussed for enhancing the bioavailability and efficacy of these compounds. The evidence suggests that pharmacological or natural induction of autophagy may alleviate neurodegenerative pathology, though context- and stage-specific modulation is essential. This work underscores the therapeutic promise of autophagy-enhancing bioactives and calls for further research into their clinical applications.
    Keywords:  Neurodegenerative disorders; alzheimer’s disease; amyotrophic lateral sclerosis; autophagy; bioactive compounds.; parkinson’s disease
    DOI:  https://doi.org/10.2174/011570159X408653251130061347
  9. Sci Adv. 2026 Mar 27. 12(13): eaeb1174
      Mitochondrial dysfunction and dysregulated proteolysis drive Huntington's disease (HD), tauopathy, and related neurodegenerative disorders. Calpain-2, a Ca2+-activated protease restrained by calpastatin (CAST), is pathologically overactivated, yet no therapies directly target this axis. We identify A36, a brain-penetrant small molecule derived from CHIR99021 that selectively stabilizes the CAST-calpain-2 complex without inhibiting GSK3. A36 acts as a protein-protein interaction stabilizer, enhancing CAST-calpain-2 binding, preventing CAST degradation, and thereby limiting calpain-2 activation and mitochondrial damage. In patients with HD induced pluripotent stem cell-derived neurons and mutant mouse striatal neurons, A36 normalized mitochondrial morphology and membrane potential, reduced oxidative stress, and improved survival. In vivo, A36 displayed favorable pharmacokinetics and central nervous system exposure; treatment reduced striatal neurodegeneration, mutant huntingtin aggregation, and motor deficits in HD R6/2 mice, and lowered phosphorylated tau, neuroinflammation, and cognitive decline in tauopathy PS19 mice. These findings establish pharmacological stabilization of CAST-calpain-2 as a therapeutic strategy and position A36 as a mechanism-selective modulator with broad neurodegenerative disease potential.
    DOI:  https://doi.org/10.1126/sciadv.aeb1174
  10. Protein Cell. 2026 Mar 25. pii: pwag026. [Epub ahead of print]
      Neurons face a fundamental proteostasis challenge: synapses and axons located far from the soma must rapidly remodel their proteome during activity, stress, and development. While local protein synthesis has long been recognized as essential for meeting these demands, classical models largely focused on ribonucleoprotein (RNP) granules as autonomous carriers of translationally silent mRNAs, treating membranous organelles as parallel logistics or metabolic systems. Recent work overturns this view, revealing that endosomes, lysosomes, axonal endoplasmic reticulum, mitochondria, and their contact sites actively function as mobile translation platforms. In this review, we propose an RBP-centered framework in which phase-separated condensates physically tether specific mRNA cohorts to organelle surfaces, coupling mRNA transport, translational control, and organelle dynamics into a unified network. By organizing recent discoveries into functional modules-long-range transport, localized translation, and stress buffering-this neuron-focused framework identifies organelle-anchored translation factories as a unifying principle of synaptic proteostasis and a broadly applicable design paradigm for highly polarized cells.
    Keywords:  RNA-binding proteins; neuronal local translation; organelle-anchored translation; ribonucleoprotein granules
    DOI:  https://doi.org/10.1093/procel/pwag026
  11. PLoS Biol. 2026 Mar;24(3): e3003697
      In some neurodegenerative diseases, the protein TDP-43 is both lost from the nucleus and forms clumps in the cytoplasm. These two pathologies can be challenging to model, but a study in PLOS Biology presents a new system that captures both features.
    DOI:  https://doi.org/10.1371/journal.pbio.3003697
  12. Elife. 2026 Mar 27. pii: RP104006. [Epub ahead of print]14
      Psilocybin is studied as innovative medication in anxiety, substance abuse and treatment-resistant depression. Animal studies show that psychedelics promote neuronal plasticity by strengthening synaptic responses and protein synthesis. However, the exact molecular and cellular changes induced by psilocybin in the human brain are not known. Here, we treated human cortical neurons derived from induced pluripotent stem cells with the 5-HT2A receptor agonist psilocin - the psychoactive metabolite of psilocybin. We analyzed how exposure to psilocin affects gene expression, neuronal morphology, synaptic markers and neuronal function. Psilocin provoked a 5-HT2A-R-mediated augmentation of BDNF abundance. Transcriptomic profiling identified gene expression signatures priming neurons to neuroplasticity. On a morphological level, psilocin induced enhanced neuronal complexity and increased expression of synaptic proteins, in particular in the postsynaptic compartment. Consistently, we observed an increased excitability and enhanced synaptic network activity in neurons treated with psilocin. In conclusion, exposure of human neurons to psilocin might induce a state of enhanced neuronal plasticity, which could explain why psilocin is beneficial in the treatment of neuropsychiatric disorders where synaptic dysfunctions are discussed.
    Keywords:  5-HT2A receptor; BDNF; Psilocin; Psychedelics; human; human induced pluripotent stem cell-derived cortical neurons; neuroplasticity; neuroscience
    DOI:  https://doi.org/10.7554/eLife.104006
  13. Expert Opin Drug Discov. 2026 Mar 24. 1-21
       INTRODUCTION: Amyotrophic Lateral Sclerosis (ALS) is the most common adult motor neuron disease, now viewed as a spectrum disorder rather than a single entity. Because of the significant person-to-person variability in the disease's biology, driven by both genetic and environmental interactions, finding a single "magic bullet" drug is unlikely. Despite decades of research, only a few ALS drugs have being developed. Drug discovery has a 95% failure rate due to genetic complexity, lack of sensitive biomarkers, diagnostic delays, inadequate animal models, and poor clinical trial design.
    AREAS COVERED: This article considers several aspects related to the prevalence of intrinsic disorder in ALS-related proteins and highlights how these features might hinder rational structure-based drug discovery.
    EXPERT OPINION: There is a common oversight in current drug discovery methodologies, which is the neglect of intrinsically disordered proteins (IDPs) playing several crucial roles in the pathology of neurodegeneration in general and ALS in particular. Therefore, it seems that the 'one-size-fits-all' approach to ALS is hitting a wall because these 'shapeshifters' of the cellular world are ignored. Consequently, to be more successful in finding drugs treating ALS, gears should be shifted from rational structure-based models to intrinsic disorder-centric approaches.
    Keywords:  Amyotrophic lateral sclerosis; binding pocket; induced folding; intrinsically disordered protein; liquid-liquid phase separation; post-translational modifications; protein-cloud; protein-protein interaction
    DOI:  https://doi.org/10.1080/17460441.2026.2648612
  14. Protein Sci. 2026 Apr;35(4): e70535
      Protein misfolding is linked to many neurodegenerative diseases. In some cases, misfolding can propagate through a prion-like mechanism whereby natively folded molecules are converted into more copies of the misfolded isoform. Prion-like propagation of misfolding is an attractive therapeutic target, but difficulties with assaying conversion directly and simply have severely limited efforts to find drugs targeting conversion of disease-related proteins. Here, we demonstrate a scalable enzymatic assay for testing potential inhibitors of prion-like conversion in superoxide dismutase-1 (SOD1), whose misfolding is linked to amyotrophic lateral sclerosis (ALS). We tested several small-molecule inhibitors of SOD1 aggregation to determine if they also inhibited prion-like conversion. We found that some compounds, like telbivudine and cisplatin, did indeed significantly delay conversion, but others, like baicalein and quercetin, had little effect. Surprisingly, some compounds, like two statins tested, actually accelerated conversion, suggesting that they might act to promote ALS progression. These results underline the fact that conversion and aggregation are distinct biophysical processes. The ability of the assay to identify compounds effective at delaying prion-like conversion holds out promise for applications in future drug discovery efforts that target propagated misfolding specifically.
    Keywords:  amyotrophic lateral sclerosis; prion‐like conversion; small‐molecule inhibitors; superoxide dismutase 1
    DOI:  https://doi.org/10.1002/pro.70535
  15. Am J Hum Genet. 2026 Mar 25. pii: S0002-9297(26)00110-2. [Epub ahead of print]
      BLOC1S1 encodes a subunit shared by the BLOC-1 and BLOC-one-related complex (BORC) hetero-octameric complexes that regulate various endolysosomal processes. Here, we report the identification of seven distinct variants in BLOC1S1 in 11 individuals from seven independent families presenting with early psychomotor delay, hypotonia, spasticity, epileptic encephalopathy, optic atrophy, and leuko-axonopathy with hypomyelination. A subset of the affected individuals also have features of hypopigmentation and ocular albinism that are similar, although milder, than those of individuals with BLOC-1-related Hermansky-Pudlak syndrome. Functional analyses show that BLOC1S1 knockout (KO) impairs the anterograde transport of lysosomes and autophagy in both non-neuronal cells and induced pluripotent stem cell (iPSC)-derived neurons. Transfection experiments reveal that most BLOC1S1 variants exhibit reduced expression, decreased assembly with other BORC/BLOC-1 subunits, and/or impaired restoration of lysosome transport and autophagy in BLOC1S1-KO cells. Additionally, we show that KO of BLOC1S1 reduces pigmentation in a melanocytic cell line and that five of the BLOC1S1 variants partially or fully restore pigmentation. These findings provide genetic, clinical, and functional evidence that loss of function (LoF) of BLOC1S1 leads to more pronounced deficits in BORC than BLOC-1 function. We conclude that the bi-allelic BLOC1S1 variants characterized here primarily result in a neurological disorder with prominent leukodystrophy, similar to the recently reported condition caused by variants in the BORCS8 subunit of BORC. Together, these findings establish BORCopathies as a distinct disease entity.
    Keywords:  BLOC-1; BLOC1S1; BORC; autophagy; leukodystrophy; lysosomes; neurodevelopmental disorder
    DOI:  https://doi.org/10.1016/j.ajhg.2026.02.024
  16. FEBS J. 2026 Mar 24.
      Redistribution of sterols among cellular compartments is crucial for the proper functions of different organelles, but how sterols are transported in plants is barely studied. Here, we identified that Arabidopsis C2 and GRAM domain-containing proteins C2GR1/2, a specialized subgroup of the lipid transfer proteins anchored at membrane contact sites (LAMs), transport sterols between membranes via their first START-like domains (SLD1s), while the SLD2 domains are inactive. Structural studies on C2GR2-SLD1/SLD2 elucidated that the sterol transport process involves the exchange of sterol and water, which requires the proper size and the amphiphilic nature of the cavity, as well as the conformational changes of the three Ω loops at the entrance. Importantly, the amphiphilicity of the cavity is shared by other SLD domains in yeast and mammals, a feature that was overlooked by previous studies. These findings not only advance our understanding of sterol transport in plants but also redefine the sterol transport paradigm for LAM proteins.
    Keywords:  C2 and GRAM containing protein; START‐like domain; amphiphilic cavity; sterol transport; structural basis
    DOI:  https://doi.org/10.1111/febs.70506
  17. bioRxiv. 2026 Mar 17. pii: 2026.03.13.711544. [Epub ahead of print]
      Restoring function to injured axons requires not only regeneration, but also accurate guidance and synapse reformation. Our understanding of how regenerating axons navigate the mature nervous system remains limited, as growth cones confront a cellular and molecular landscape distinct from development. Using Caenorhabditis elegans , we found that the basement membrane protein Nidogen (NID-1) promotes local guidance of regenerating motor axons in the mature nervous system by facilitating their growth alongside neighboring intact neuronal processes. Regenerating cholinergic axons preferentially track the branched dendrites of the PVD mechanosensory neuron or, in the absence of PVD dendrites, are guided alongside GABAergic commissures instead. Loss of nid-1 disrupts this guidance, reducing axon-PVD colocalization, increasing displacement from the pre-injury point of contact with the dorsal nerve cord, and disrupting synapse reformation and functional recovery. Tissue-specific rescue indicates that NID-1 expressed by body wall muscles or the hypodermis is sufficient to guide regenerating axons, whereas muscle-derived NID-1 is required to restore synapse reformation. Genetic data indicate that NID-1 function guides regenerating axons in coordination with laminin and integrin. Although this complex primarily directs cholinergic motor axons, ectopic integrin expression in GABAergic neurons is sufficient to reroute their regenerating axons alongside PVD dendrites in a NID-1-dependent manner. Together, these findings identify a NID-1-dependent post-developmental mechanism for directing regenerating axons and promoting functional repair.
    DOI:  https://doi.org/10.64898/2026.03.13.711544
  18. Cell. 2026 Mar 23. pii: S0092-8674(26)00233-3. [Epub ahead of print]
      Neurodegenerative diseases (NDs) pose clinical challenges due to their complexity and molecular heterogeneity. Here, we present a pan-neurodegeneration atlas (PanNDA) from multilayer, deep proteomic analysis of 2,279 human brain samples spanning 6 major NDs: Alzheimer's disease (AD), Lewy body dementia (LBD), frontotemporal lobar degeneration with TDP-43 pathology, progressive supranuclear palsy with tau pathology, vascular dementia, and Parkinson's disease. PanNDA integrates data from whole proteome, detergent-insoluble proteome, and posttranslational modifications (phosphorylation and ubiquitination), enabling intra- and inter-disease comparisons. Intra-disease analyses uncover distinct molecular subtypes (e.g., three in AD and four in LBD), reveal dysregulated pathways, and prioritize top-ranked proteins. Inter-disease comparisons identify shared alterations in NDs, such as GPNMB in microglial and lysosomal activation and NPTX2 in synaptic regulation, alongside disease-specific changes and hub regulators within protein networks. Overall, PanNDA provides a systems-level framework for understanding ND mechanisms and serves as a foundational resource that is accessible via an interactive website: https://penglab.shinyapps.io/pannda.
    Keywords:  Alzheimer's disease; Lewy body dementia; Parkinson’s disease; frontotemporal lobar degeneration; mass spectrometry; neurodegenerative diseases; posttranslational modifications; progressive supranuclear palsy; proteomics; vascular dementia
    DOI:  https://doi.org/10.1016/j.cell.2026.02.026
  19. Methods Enzymol. 2026 ;pii: S0076-6879(26)00009-1. [Epub ahead of print]728 183-209
      Intracellular sterol transport proteins (STPs) are key regulators of cholesterol homeostasis and potential drug targets in a broad range of diseases including atherosclerosis, infectious diseases and cancer. Therefore, the ability to rapidly identify and validate small molecule inhibitors of these transporters is of great significance. In this chapter, we outline a series of biophysical and biochemical assays of increasing complexity to screen small molecules for inhibition of STPs in medium-to-high throughput. These include differential scanning fluorimetry to determine compound binding, competitive fluorescence polarization assays employing fluorescent sterols as tracers, and FRET-based lipid transport assays in synthetic liposomes. As these assays are now established for the majority of human STPs, compounds can also directly be profiled for selectivity across structurally and functionally related targets.
    Keywords:  Cholesterol; Differential scanning fluorimetry; FRET; Fluorescence polarization; Inhibitors; Sterol transport protein
    DOI:  https://doi.org/10.1016/bs.mie.2026.01.009
  20. Int J Mol Sci. 2026 Mar 10. pii: 2550. [Epub ahead of print]27(6):
      Neuronal function relies on the precise coordination between intracellular calcium (Ca2+) signaling and the cytoskeletal architecture that underpins synaptic transmission, plasticity, and structural stability. Disruption of this calcium-cytoskeleton interplay has been noted in numerous neurodegenerative diseases. We discuss how Ca2+-dependent cytoskeletal remodeling governs long-term potentiation and depression, dendritic spine morphology, and presynaptic function, highlighting the functions of end-binding proteins, STIM (Stromal Interaction Molecule)/Orai-mediated store-operated calcium entry, and the spine apparatus. Disease-specific manifestations of cytoskeletal-calcium dysregulation are reviewed across Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, tauopathies, and prion disorders. Finally, we evaluate emerging therapeutic strategies targeting calcium homeostasis, cytoskeletal dynamics, and their downstream effectors, including multi-target approaches.
    Keywords:  Alzheimer’s disease; cytoskeleton neurodegeneration; dendritic spines; dynamic tubulin microtubules; spine apparatus
    DOI:  https://doi.org/10.3390/ijms27062550
  21. Cell Death Dis. 2026 Mar 27.
      Huntington's Disease (HD) is characterized by progressive motor and cognitive decline, largely driven by cortico-striatal synaptic dysfunction. Central to these processes is huntingtin (HTT) protein, which is abundantly present at the synapse. HTT regulates the synaptic vesicle cycle at presynaptic terminals and serves as a scaffold at the postsynaptic density where it modulates receptor dynamics. An expanding network of HTT-interacting proteins (HIPs), crucial for maintaining synaptic structure and function, underscores the role of HTT as a core component of synaptic integrity. This review examines the 30-year research journey that has unveiled HTT pre- and postsynaptic partners, with focus on experimentally validated interactors and their involvement in HD cortico-striatal synaptic dysfunction.
    DOI:  https://doi.org/10.1038/s41419-026-08584-6
  22. Methods Enzymol. 2026 ;pii: S0076-6879(26)00033-9. [Epub ahead of print]728 369-387
      Lipids regulate a broad spectrum of cellular functions through spatiotemporally controlled lipid-protein interactions. Dysregulation of lipid metabolism and lipid-mediated signaling is associated with diverse human diseases, including cancer, metabolic disorders, and neurodegenerative conditions. Consequently, selective inhibition of site-specific lipid-protein interactions has emerged as a promising therapeutic strategy to modulate aberrant cell signaling at the membrane interface. Here, we present a streamlined, quantitative workflow for the discovery, characterization, and evaluation of small-molecule inhibitors that disrupt lipid-dependent membrane association and activation of cytosolic signaling proteins. The protocol integrates a high-throughput fluorescence-quenching assay for inhibitor screening, detailed biochemical and cellular target-validation methods, and standardized procedures for in vitro and in vivo assessment of inhibitor potency, specificity, and safety. These general protocols provide a versatile and reproducible platform for developing potent, specific, and mechanistically defined inhibitors targeting a wide range of lipid-binding proteins implicated in disease.
    Keywords:  Cancer; Lipid signaling; Lipid-protein interaction, high-throughput screening; Small molecule inhibitors
    DOI:  https://doi.org/10.1016/bs.mie.2026.01.025