bims-lypmec Biomed News
on Lysosomal positioning and metabolism in cardiomyocytes
Issue of 2025–06–15
seven papers selected by
Satoru Kobayashi, New York Institute of Technology



  1. Pain Rep. 2025 Aug;10(4): e1282
      Lysosomes are recycling centers of nearly all types of eukaryotic cells. Lysosomal ion channels maintain ion homeostasis of lysosomes and exchange ions with neighboring cytoplasm and subcellular structures. In these ways, lysosomal ion channels contribute to major function of lysosomes such as autophagy and lysosomal exocytosis. Deficiency in some lysosomal ion channels results in lysosome storage disorders such as mucolipidosis IV that is associated with early-onset neurodegeneration. Moreover, lysosomal ion channels are involved in a variety of conditions such as cancer, infectious diseases, respiratory diseases, cardiovascular and kidney diseases. This narrative review aims to summarize current evidence that supports the potential role of lysosomal ion channels in pain. Lysosomal P2X4 may contribute to pain through trafficking to plasma membrane as well as lysosomal exocytosis. In dorsal root ganglion neurons, lysosomal TRPM8 functions as a constitutive supply from lysosomal to plasma membrane, whereas lysosomal TRPA1 may mediate vehicle exocytosis of neurotransmitters. Moreover, recent studies suggest that Tmem63A forms a mechanosensory ion channel in lysosomal membrane and that Tmem63A of dorsal root ganglion neurons contributes to mechanical hypersensitivity in chronic pain models. Furthermore, evidences indicating a potential role of TRPMLs in pain include ROS sensitivity of TRPML1, chemokine release mediated by TRPML2, and re-expression of TRPML3 upon nerve injury. However, despite the current supporting evidence, the role of lysosomal ion channels in pain is just being explored, and future studies are needed to address the significance, mechanism, and potential translation of lysosomal ion channels in pain.
    Keywords:  Lysosomal ion channels; P2X4; Pain; TRPM8; Tmem63A
    DOI:  https://doi.org/10.1097/PR9.0000000000001282
  2. Life Sci Alliance. 2025 Aug;pii: e202403015. [Epub ahead of print]8(8):
      Immune cells migrate via actomyosin contractility mediated by myosin IIA activation, wherein the lysosomal Ragulator complex-MPRIP interaction is crucial. However, the precise mechanism underlying lysosome-mediated myosin IIA activation has not been elucidated. Here, we found that calcium efflux from the lysosomal TRPML1 channel promotes leukocyte trafficking by enhancing the interaction between the Ragulator complex and MPRIP. Disrupting the lysosome-anchoring site of Lamtor1 impaired the localization of the Ragulator complex to lysosomes, diminishing the TRPML1-mediated leukocyte migration and interaction between Lamtor1 and MPRIP. Furthermore, ouabain, a cardiac glycoside, dissociated Lamtor1 from lysosomes, inhibiting the interaction between the Ragulator complex and myosin IIA activation, thereby suppressing cell migration. Therapeutically, ouabain ameliorated the severity of MSU-induced gouty arthritis and LPS-induced lung injury in mice by inhibiting leukocyte infiltration. Overall, lysosomes facilitate the interaction between the Ragulator complex and MPRIP by supplying calcium ions through TRPML1 channels, thereby activating myosin IIA and promoting leukocyte migration.
    DOI:  https://doi.org/10.26508/lsa.202403015
  3. Cell Rep. 2025 Jun 10. pii: S2211-1247(25)00600-X. [Epub ahead of print]44(6): 115829
      Lifestyle diseases, such as obesity, diabetes, and metabolic syndrome, are leading health problems, most of which are related to abnormal lipid metabolism. Lysosomes can degrade lipid droplets (LDs) via microautophagy, but the regulatory factors and physiological significance of this process are not fully understood. Here, we report the molecular mechanism and pathophysiological roles of microlipophagy, regulated by the lysosomal membrane protein LAMP2B. Our study reveals that LAMP2B interacts with phosphatidic acid, facilitating lysosomal-LD interactions and enhancing lipid hydrolysis via microlipophagy depending on endosomal sorting complexes required for transport. Correlative light and electron microscopy demonstrates direct LD uptake into lysosomes at contact sites. Moreover, LAMP2B overexpression in mice prevents high-fat diet-induced obesity, insulin resistance, and adipose tissue inflammation; liver lipidomics analysis suggests enhanced triacylglycerol hydrolysis. Overall, the findings of this study elucidate the mechanism of microlipophagy, which could be promising for the treatment of obesity and related disorders.
    Keywords:  CP: Cell biology; CP: Metabolism; LAMP2B; lipid droplet; lysosome; microautophagy; microlipophagy
    DOI:  https://doi.org/10.1016/j.celrep.2025.115829
  4. Prog Lipid Res. 2025 Jun 05. pii: S0163-7827(25)00023-2. [Epub ahead of print]99 101341
      Age-related neurodegenerative disorders are often associated with disruptions in lipid metabolism. A critical aspect is the impairment of the interaction between lipid droplets (LDs) and lysosomal function, leading to the accumulation of toxic lipid species. This accumulation triggers cellular stress, inflammation, and defective waste processing within cells, disrupting cellular homeostasis and amplifying neuroinflammatory processes. Recent studies have shown that alterations in phospholipid and fatty acid homeostasis drive neuroinflammation and oxidative stress, exacerbating neurodegenerative processes. This review focuses on the role of neuropathy target esterase (PNPLA6/NTE) and NTE-related esterase (PNPLA7/NRE) in lipid metabolism, highlighting how dysregulation of these enzymes contributes to neurodegeneration, inflammation, and lysosomal dysfunction. Additionally, we discuss the involvement of lipid rafts, sphingolipids, and phospholipase enzymes, particularly PLA2 family members, in cellular signaling and membrane dynamics. By examining the relationship between lipid metabolism, inflammatory signaling, and lysosomal storage disorders, we aim to provide a comprehensive understanding of how LDs and lysosomes interact to influence cellular homeostasis in neurodegenerative conditions, which could lead to new therapeutic strategies addressing lipid dysregulation in age-related neurological disorders.
    Keywords:  Fatty acids; Inflammaging; Lipid droplets; Lipid membranes; Lysosomes; PNPLA6/NTE
    DOI:  https://doi.org/10.1016/j.plipres.2025.101341
  5. Sci Signal. 2025 Jun 10. 18(890): eadt1936
      Lysosomes are versatile organelles that play pivotal roles in cellular recycling and signal transduction. They are crucial for the autophagic degradation and recycling of macromolecules, which facilitates the efficient turnover of cellular components. Beyond their intracellular roles, lysosomes also regulate the degradation and assembly of extracellular matrix (ECM) constituents, affecting ECM remodeling and the processing of signaling molecules essential for cellular communication and adaptation to the microenvironment. Conversely, the ECM regulates key lysosomal functions, including biogenesis, acidification, and subcellular positioning. In this Review, we discuss the bidirectional interaction between lysosomes and the ECM and explore its implications in the development and treatment of neurodegenerative disease.
    DOI:  https://doi.org/10.1126/scisignal.adt1936
  6. Bioconjug Chem. 2025 Jun 11.
      Iron is crucial for numerous biological processes, and lysosomes play an essential role in iron metabolism by regulating Fe3+ levels. Disruptions of this regulation can lead to Fe3+ accumulation, resulting in membrane damage and ferroptosis. Here, we have developed a water-soluble fluorescent probe BiNIT that specifically targets lysosomes for the selective detection of Fe3+. BiNIT features a bis-naphthalimide structure linked by a thiophene moiety and incorporates two quaternary ammonium groups, which enhance its ability to target lysosomes and its solubility in aqueous environments. The probe showed high selectivity for Fe3+, with fluorescence quenching resulting from the paramagnetism of Fe3+ and its capacity to induce probe aggregation. This aggregation occurs through coordination bonds between Fe3+ and the carbonyl oxygen, imide nitrogen, or thiophene sulfur in multiple probe molecules. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) confirmed the formation of nanoparticles upon Fe3+ binding. Moreover, BiNIT remains stable in environments with pH values above 4, facilitating precise monitoring of Fe3+ levels within lysosomes. This innovative tool provides valuable insights into iron homeostasis, oxidative stress, and ferroptosis, aiding research on iron-related diseases and the development of therapeutic strategies.
    DOI:  https://doi.org/10.1021/acs.bioconjchem.5c00092
  7. J Mol Cell Cardiol Plus. 2025 Jun;12 100453
      Type 2 diabetes (T2D) and obesity strongly lead to diabetic cardiomyopathy (DCM). The involvement of mitochondria-associated reticular membranes (MAMs), a signaling hub in the cardiomyocyte, starts to be demonstrated in T2D-related metabolic disorders. We recently discovered a cardiac MAM Ca2+ uncoupling in a high-fat high-sucrose diet (HFHSD)-induced mouse model of DCM. To better determine the role of MAMs in the progression of DCM, we here aimed to characterize the proteomic composition and function of the cardiac MAMs of another obesogenic T2D mouse model, the leptin-deficient ob/ob mouse. 12-week old male C57Bl6-N ob/ob mice displayed strain rate dysfunction and concentric remodeling, while no change was observed in fractional shortening or diastolic function. Increased lipid deposition but no fibrosis was measured in the ob/ob heart compared to WT. Electron microscopy analysis revealed that cardiac MAM length and width were similar between both groups. A trend towards an increased MAM protein content was measured in the ob/ob heart. MAM proteome analyses showed mainly increased processes in ob/ob hearts: cellular response to stress, lipid metabolism, ion transport and membrane organization. Functionally, MAM-driven Ca2+ fluxes were unchanged but hypoxic stress induced a cell death increase in the ob/ob cardiomyocyte. Mitochondrial respiration, cardiomyocyte shortening, ATP and ROS content were similar between groups. To conclude, at that age, while being strongly hyperglycemic and insulin-resistant, the ob/ob mouse model rather displays a modest DCM without strong changes in MAMs: preserved structural and functional MAM Ca2+ coupling but increased response to stress.
    Keywords:  Database; Diabetic cardiopathy; ERMCs; MERCs; Mitochondrial calcium uniporter; SR-mitochondria coupling
    DOI:  https://doi.org/10.1016/j.jmccpl.2025.100453