[ad_1]
Ballabio, A. & Bonifacino, J. S. Lysosomes as dynamic regulators of cell and organismal homeostasis. Nat. Rev. Mol. Cell Biol. 21, 101–118 (2020).
Medoh, U. N., Chen, J. Y. & Abu-Remaileh, M. Classes from metabolic perturbations in lysosomal storage issues for neurodegeneration. Curr. Opin. Syst. Biol. 29, 100408 (2022).
Platt, F. M., d’Azzo, A., Davidson, B. L., Neufeld, E. F. & Tifft, C. J. Lysosomal storage illnesses. Nat. Rev. Dis. Primers 4, 27 (2018).
Ferguson, S. M. Neuronal lysosomes. Neurosci. Lett. 697, 1–9 (2019).
Perera, R. M. & Zoncu, R. The lysosome as a regulatory hub. Annu. Rev. Cell Dev. Biol. 32, 223–253 (2016).
Savini, M., Zhao, Q. & Wang, M. C. Lysosomes: signaling hubs for metabolic sensing and longevity. Traits Cell Biol. 29, 876–887 (2019).
Ballabio, A. & Gieselmann, V. Lysosomal issues: from storage to mobile injury. Biochim. Biophys. Acta 1793, 684–696 (2009).
Boustany, R. M. Lysosomal storage illnesses—the horizon expands. Nat. Rev. Neurol. 9, 583–598 (2013).
Marques, A. R. A. & Saftig, P. Lysosomal storage issues—challenges, ideas and avenues for remedy: past uncommon illnesses. J. Cell Sci. 132, jcs221739 (2019).
Wallings, R. L., Humble, S. W., Ward, M. E. & Wade-Martins, R. Lysosomal dysfunction on the centre of Parkinson’s illness and frontotemporal dementia/amyotrophic lateral sclerosis. Traits Neurosci. 42, 899–912 (2019).
Wang, C., Telpoukhovskaia, M. A., Bahr, B. A., Chen, X. & Gan, L. Endo-lysosomal dysfunction: a converging mechanism in neurodegenerative illnesses. Curr. Opin. Neurobiol. 48, 52–58 (2018).
Abu-Remaileh, M. et al. Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes. Science 358, 807–813 (2017).
Thai, T. H. et al. Regulation of the germinal heart response by microRNA-155. Science 316, 604–608 (2007).
Pisoni, R. L., Acker, T. L., Lisowski, Ok. M., Lemons, R. M. & Thoene, J. G. A cysteine-specific lysosomal transport system gives a significant route for the supply of thiol to human fibroblast lysosomes: attainable function in supporting lysosomal proteolysis. J. Cell Biol. 110, 327–335 (1990).
Eiberg, H., Gardiner, R. M. & Mohr, J. Batten illness (Spielmeyer-Sjogren illness) and haptoglobins (HP): indication of linkage and project to chr. 16. Clin. Genet. 36, 217–218 (1989).
Lerner, T.J. et al. Isolation of a novel gene underlying Batten illness, CLN3. Cell 82, 949–957 (1995).
Mirza, M. et al. The CLN3 gene and protein: what we all know. Mol. Genet. Genomic Med. 7, e859 (2019).
Butz, E. S., Chandrachud, U., Mole, S. E. & Cotman, S. L. Transferring in direction of a brand new period of genomics within the neuronal ceroid lipofuscinoses. Biochim. Biophys. Acta Mol. Foundation Dis. 1866, 165571 (2019).
Jarvela, I. et al. Biosynthesis and intracellular focusing on of the CLN3 protein faulty in Batten illness. Hum. Mol. Genet. 7, 85–90 (1998).
Storch, S., Pohl, S. & Braulke, T. A dileucine motif and a cluster of acidic amino acids within the second cytoplasmic area of the batten disease-related CLN3 protein are required for environment friendly lysosomal focusing on. J. Biol. Chem. 279, 53625–53634 (2004).
Mao, Q., Foster, B. J., Xia, H. & Davidson, B. L. Membrane topology of CLN3, the protein underlying Batten illness. FEBS Lett. 541, 40–46 (2003).
Ezaki, J. et al. Characterization of Cln3p, the gene product chargeable for juvenile neuronal ceroid lipofuscinosis, as a lysosomal integral membrane glycoprotein. J. Neurochem. 87, 1296–1308 (2003).
Oetjen, S., Kuhl, D. & Hermey, G. Revisiting the neuronal localization and trafficking of CLN3 in juvenile neuronal ceroid lipofuscinosis. J. Neurochem. 139, 456–470 (2016).
Perland, E., Bagchi, S., Klaesson, A. & Fredriksson, R. Traits of 29 novel atypical solute carriers of main facilitator superfamily kind: evolutionary conservation, predicted construction and neuronal co-expression. Open Biol. 7, 170142 (2017).
Mitchison, H. M. et al. Focused disruption of the Cln3 gene gives a mouse mannequin for Batten illness. The Batten Mouse Mannequin Consortium [corrected]. Neurobiol. Dis. 6, 321–334 (1999).
Kovacs, A. D. & Pearce, D. A. Discovering probably the most applicable mouse mannequin of juvenile CLN3 (Batten) illness for therapeutic research: the significance of genetic background and gender. Dis. Mannequin. Mech. 8, 351–361 (2015).
Lojewski, X. et al. Human iPSC fashions of neuronal ceroid lipofuscinosis seize distinct results of TPP1 and CLN3 mutations on the endocytic pathway. Hum. Mol. Genet. 23, 2005–2022 (2014).
Platt, F. M. Sphingolipid lysosomal storage issues. Nature 510, 68–75 (2014).
Fuller, M. & Futerman, A. H. The mind lipidome in neurodegenerative lysosomal storage issues. Biochem. Biophys. Res. Commun. 504, 623–628 (2018).
Hobert, J. A. & Dawson, G. A novel function of the Batten illness gene CLN3: affiliation with BMP synthesis. Biochem. Biophys. Res. Commun. 358, 111–116 (2007).
Padilla-Lopez, S., Langager, D., Chan, C. H. & Pearce, D. A. BTN1, the Saccharomyces cerevisiae homolog to the human Batten illness gene, is concerned in phospholipid distribution. Dis. Mannequin. Mech. 5, 191–199 (2012).
Kopp, F. et al. The glycerophospho metabolome and its affect on amino acid homeostasis revealed by mind metabolomics of GDE1(−/−) mice. Chem. Biol. 17, 831–840 (2010).
Allen, F., Pon, A., Wilson, M., Greiner, R. & Wishart, D. CFM-ID: an internet server for annotation, spectrum prediction and metabolite identification from tandem mass spectra. Nucleic Acids Res. 42, W94–W99 (2014).
Sumner, L. W. et al. Proposed minimal reporting requirements for chemical evaluation Chemical Evaluation Working Group (CAWG) Metabolomics Requirements Initiative (MSI). Metabolomics 3, 211–221 (2007).
Dang Do, A. N. et al. Neurofilament gentle chain ranges correlate with scientific measures in CLN3 illness. Genet. Med. 23, 751–757 (2021).
Fowler, S. & De Duve, C. Digestive exercise of lysosomes. 3. The digestion of lipids by extracts of rat liver lysosomes. J. Biol. Chem. 244, 471–481 (1969).
Schmidtke, C. et al. Lysosomal proteome evaluation reveals that CLN3-defective cells have a number of enzyme deficiencies related to modifications in intracellular trafficking. J. Biol. Chem. 294, 9592–9604 (2019).
Corda, D. et al. The rising physiological roles of the glycerophosphodiesterase household. FEBS J. 281, 998–1016 (2014).
Patton-Vogt, J. Transport and metabolism of glycerophosphodiesters produced by way of phospholipid deacylation. Biochim. Biophys. Acta 1771, 337–342 (2007).
Rigoni, M. et al. Equal results of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures. Science 310, 1678–1680 (2005).
Fallbrook, A., Turenne, S. D., Mamalias, N., Kish, S. J. & Ross, B. M. Phosphatidylcholine and phosphatidylethanolamine metabolites could regulate mind phospholipid catabolism through inhibition of lysophospholipase exercise. Mind Res. 834, 207–210 (1999).
Storey, J. D. A direct strategy to false discovery charges. J. R. Stat. Soc. B 64, 479–498 (2002).
Wyant, G. A. et al. NUFIP1 is a ribosome receptor for starvation-induced ribophagy. Science 360, 751–758 (2018).
Perez-Riverol, Y. et al. The PRIDE database and associated instruments and sources in 2019: enhancing assist for quantification information. Nucleic Acids Res. 47, D442–D450 (2019).
Salek, R. M., Steinbeck, C., Viant, M. R., Goodacre, R. & Dunn, W. B. The function of reporting requirements for metabolite annotation and identification in metabolomic research. Gigascience 2, 13 (2013).
Chook, S. S., Marur, V. R., Sniatynski, M. J., Greenberg, H. Ok. & Kristal, B. S. Serum lipidomics profiling utilizing LC-MS and high-energy collisional dissociation fragmentation: deal with triglyceride detection and characterization. Anal. Chem. 83, 6648–6657 (2011).
Taguchi, R. & Ishikawa, M. Exact and international identification of phospholipid molecular species by an Orbitrap mass spectrometer and automatic search engine Lipid Search. J. Chromatogr. A 1217, 4229–4239 (2010).
Yamada, T. et al. Improvement of a lipid profiling system utilizing reverse-phase liquid chromatography coupled to high-resolution mass spectrometry with fast polarity switching and an automatic lipid identification software program. J. Chromatogr. A 1292, 211–218 (2013).
Hankin, J. A., Murphy, R. C., Barkley, R. M. & Gijon, M. A. Ion mobility and tandem mass spectrometry of phosphatidylglycerol and bis(monoacylglycerol)phosphate (BMP). Int. J. Mass Spectrom. 378, 255–263 (2015).
Wang, T., Wei, J. J., Sabatini, D. M. & Lander, E. S. Genetic screens in human cells utilizing the CRISPR-Cas9 system. Science 343, 80–84 (2014).
Krink-Koutsoubelis, N. et al. Engineered manufacturing of short-chain acyl-coenzyme A esters in Saccharomyces cerevisiae. ACS Synth. Biol. 7, 1105–1115 (2018).
Zheng, B., Berrie, C. P., Corda, D. & Farquhar, M. G. GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors. Proc. Natl Acad. Sci. USA 100, 1745–1750 (2003).
[ad_2]