Defective autophagy in neurons and astrocytes from mice deficient in PI(3,5)P2

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882

Rapamycin fed late in life extends lifespan in genetically heterogeneous mice

Harrison, D. E., Strong, R., Sharp, Z. D., Nelson, J. F., Astle, C. M., Flurkey, K., Nadon, N. L., Wilkinson, J. E., Frenkel, K., Carter, C. S., et al. (2009) · Nature · doi:10.1038/nature08221 · Cited by 3,766

Loss of autophagy in the central nervous system causes neurodegeneration in mice

Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500

Protein aggregation and neurodegenerative disease

Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Sreedharan, J., Blair, I. P., Tripathi, V. B., Hu, X., Vance, C., Rogelj, B., Ackerley, S., Durnall, J. C., Williams, K. L., Buratti, E., et al. (2008) · Science · doi:10.1126/science.1154584 · Cited by 2,630

How to Interpret LC3 Immunoblotting

Mizushima, N., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4600 · Cited by 2,595

Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes

Klionsky, D. J., Abeliovich, H., Agostinis, P., Agrawal, D. K., Aliev, G., Askew, D. S., Baba, M., Baehrecke, E. H., Bahr, B. A., Ballabio, A., et al. (2008) · Autophagy · doi:10.4161/auto.5338 · Cited by 2,230

Autophagy: from phenomenology to molecular understanding in less than a decade

Klionsky, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2245 · Cited by 1,977

Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum

Axe, E. L., Walker, S. A., Manifava, M., Chandra, P., Roderick, H. L., Habermann, A., Griffiths, G., & Ktistakis, N. T. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803137 · Cited by 1,885

Astrocytes as determinants of disease progression in inherited amyotrophic lateral sclerosis

Yamanaka, K., Chun, S. J., Boillee, S., Fujimori-Tonou, N., Yamashita, H., Gutmann, D. H., Takahashi, R., Misawa, H., & Cleveland, D. W. (2008) · Nature Neuroscience · doi:10.1038/nn2047 · Cited by 1,140 · cited 1×

Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology

Suelves, N., Saleki, S., Ibrahim, T., Palomares, D., Moonen, S., Koper, M. J., Vrancx, C., Vadukul, D. M., Papadopoulos, N., Viceconte, N., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01578-x · Cited by 43

Chitotriosidase and lysosomal enzymes as potential biomarkers of disease progression in amyotrophic lateral sclerosis: A survey clinic-based study

Pagliardini, V., Pagliardini, S., Corrado, L., Lucenti, A., Panigati, L., Bersano, E., Servo, S., Cantello, R., D'Alfonso, S., & Mazzini, L. (2015) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2014.12.016 · Cited by 42

Mouse Models of PI(3,5)P2 Deficiency with Impaired Lysosome Function

Lenk, G. M., & Meisler, M. H. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-397926-1.00014-7 · Cited by 40

CRISPR knockout screen implicates three genes in lysosome function

Lenk, G. M., Park, Y. N., Lemons, R. M., Flynn, E., Plank, M., Frei, C. M., Davis, M. J., Gregorka, B., Swanson, J. A., Meisler, M. H., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45939-w · Cited by 41

Understanding the complexities of SARS-CoV2 infection and its immunology: A road to immune-based therapeutics

Kumar, V. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.106980 · Cited by 42

Minocycline is effective in intracerebral hemorrhage by inhibition of apoptosis and autophagy

Wu, Z., Zou, X., Zhu, W. P., Mao, Y. Q., Chen, L., & Zhao, F. (2016) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2016.10.025 · Cited by 37

Phosphatidylinositol Kinases and Phosphatases in Entamoeba histolytica

Nakada‐Tsukui, K., Watanabe, N., Maehama, T., & Nozaki, T. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00150 · Cited by 42

AMP‐activated protein kinase is involved in induction of protective autophagy in astrocytes exposed to oxygen‐glucose deprivation

Gabryel, B., Kost, A., Liśkiewicz, D., Liber, S., Machnik, G., Wiaderkiewicz, R., & Łabuzek, K. (2014) · Cell Biology International · doi:10.1002/cbin.10299 · Cited by 39

The role of lipids in autophagy and its implication in neurodegeneration

Hernández-Díaz, S., & Soukup, S. (2020) · Cell Stress · doi:10.15698/cst2020.07.225 · Cited by 39

PIKfyve complex regulates early melanosome homeostasis required for physiological amyloid formation

Bissig, C., Croisé, P., Heiligenstein, X., Hurbain, I., Lenk, G. M., Kaufman, E. L., Sannerud, R., Annaert, W. G., Meisler, M. H., Weisman, L. S., et al. (2019) · Journal of Cell Science · doi:10.1242/jcs.229500 · Cited by 35

Autophagy dysregulation and the fate of retinal ganglion cells in glaucomatous optic neuropathy

Russo, R., Nucci, C., Corasaniti, M. T., Bagetta, G., & Morrone, L. A. (2015) · Progress in brain research · doi:10.1016/bs.pbr.2015.04.009 · Cited by 37

C-X-C Motif Chemokine 10 Impairs Autophagy and Autolysosome Formation in Non-alcoholic Steatohepatitis

Zhang, X., Wu, W. K. K., Xu, W., Man, K., Wang, X., Han, J., Leung, W. Y., Wu, R., Liu, K., & Yu, J. Q. (2017) · Theranostics · doi:10.7150/thno.19068 · Cited by 37

Sphingosine kinase 1-associated autophagy differs between neurons and astrocytes

Moruno-Manchon, J. F., Uzor, N.-E., Ambati, C. R., Shetty, V., Putluri, N., Jagannath, C., McCullough, L. D., & Tsvetkov, A. S. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0599-5 · Cited by 36

Protein clearing pathways in ALS.

Ferrucci, M., Fulceri, F., Toti, L., Soldani, P., Siciliano, G., Paparelli, A., & Fornai, F. (2011) · PubMed · doi:10.4449/aib.v149i1.1258 · Cited by 35

Autophagy Dysfunction in ALS: from Transport to Protein Degradation

Cozzi, M., & Ferrari, V. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02029-3 · Cited by 38

PI(3,5)P2 biosynthesis regulates oligodendrocyte differentiation by intrinsic and extrinsic mechanisms

Mironova, Y. A., Lenk, G. M., Lin, J.-P., Lee, S. J., Twiss, J. L., Vaccari, I., Bolino, A., Havton, L. A., Min, S. H., Abrams, C. S., et al. (2016) · eLife · doi:10.7554/elife.13023 · Cited by 35

Protein recycling pathways in neurodegenerative diseases

Fecto, F., Esengul, Y. T., & Siddique, T. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt243 · Cited by 34

Vac14 Protein Multimerization Is a Prerequisite Step for Fab1 Protein Complex Assembly and Function

Alghamdi, T. A., Ho, C. Y., Mrakovic, A., Taylor, D. L., Mao, D. Y. L., & Botelho, R. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.453712 · Cited by 33

HIV Nef and Antiretroviral Therapy Have an Inhibitory Effect on Autophagy in Human Astrocytes that May Contribute to HIV-Associated Neurocognitive Disorders

Cheney, L., Guzik, H. M., Macaluso, F., Macián, F., Cuervo, A. M., & Berman, J. W. (2020) · Cells · doi:10.3390/cells9061426 · Cited by 34

Lysosomal activity depends on TRPML1-mediated Ca2+ release coupled to incoming vesicle fusions

Bhattacharjee, A., Abuammar, H., & Juhász, G. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107911 · Cited by 35

Phenotypic transition of corpus cavernosum smooth muscle cells subjected to hypoxia

Lv, B., Zhao, J., Yang, F., Huang, X., Chen, G., Ke-bing, Y., Liu, S., Fan, C., Fu, H., & Chen, Z.-D. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1902-0 · Cited by 31

TRPMLs and TPCs: targets for lysosomal storage and neurodegenerative disease therapy?

Krogsaeter, E., Rosato, A. S., & Grimm, C. (2022) · Cell Calcium · doi:10.1016/j.ceca.2022.102553 · Cited by 31

Pathomechanism Heterogeneity in the Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Disease Spectrum: Providing Focus Through the Lens of Autophagy

Casterton, R., Hunt, R. J., & Fanto, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.018 · Cited by 34

Fig4 deficiency: A newly emerged lysosomal storage disorder?

Martyn, C. P., & Li, J. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.11.001 · Cited by 31

Cerebral hypomyelination associated with biallelic variants of FIG4

Lenk, G. M., Berry, I. R., Stutterd, C., Blyth, M., Green, L., Vadlamani, G., Warren, D., Craven, I., Fanjul‐Fernández, M., Rodriguez‐Casero, V., et al. (2019) · Human Mutation · doi:10.1002/humu.23720 · Cited by 29

Emerging Human Coronavirus Infections (SARS, MERS, and COVID-19): Where They Are Leading Us

Kumar, V. (2020) · International Reviews of Immunology · doi:10.1080/08830185.2020.1800688 · Cited by 29

Activated Endolysosomal Cation Channel TRPML1 Facilitates Maturation of α-Synuclein-Containing Autophagosomes

Pollmanns, M. R., Beer, J., Rosignol, I., Rodríguez‐Muela, N., Falkenburger, B. H., & Dinter, E. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.861202 · Cited by 27

Identification and characterization of splicing variants of PLEKHA5 (Plekha5) during brain development

Yamada, K., Nomura, N., Arisa, Y., Yamada, Y., & Wakamatsu, N. (2011) · Gene · doi:10.1016/j.gene.2011.10.018 · Cited by 25

Minocycline induces protective autophagy in vascular endothelial cells exposed to an in vitro model of ischemia/reperfusion-induced injury

DONG, W., XIAO, S., CHENG, M., Ye, X., & Zheng, G. (2015) · Biomedical Reports · doi:10.3892/br.2015.554 · Cited by 24

PIKfyve regulates melanosome biogenesis

Liggins, M. C., Flesher, J. L., Jahid, S., Vasudeva, P., Eby, V., Takasuga, S., Sasaki, J., Sasaki, T., Boissy, R. E., & Ganesan, A. K. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007290 · Cited by 23

Prospects for gene replacement therapies in amyotrophic lateral sclerosis

Giovannelli, I., Higginbottom, A., Kirby, J., Azzouz, M., & Shaw, P. J. (2022) · Nature Reviews Neurology · doi:10.1038/s41582-022-00751-5 · Cited by 23

Dynamic control of neuroexocytosis by phosphoinositides in health and disease

Wen, P. J., Osborne, S. L., & Meunier, F. A. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.08.001 · Cited by 23

The Sac domain-containing phosphoinositide phosphatases: structure, function, and disease

Hsu, F., & Mao, Y. (2013) · Frontiers in Biology · doi:10.1007/s11515-013-1258-y · Cited by 21

Held Up in Traffic—Defects in the Trafficking Machinery in Charcot-Marie-Tooth Disease

Markworth, R., Bähr, M., & Burk, K. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.695294 · Cited by 20

Lysosomal TRPML1 Channel: Implications in Cardiovascular and Kidney Diseases

Li, G., & Li, P. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-4254-8_13 · Cited by 22

Amyotrophic lateral sclerosis (ALS) and the endocrine system: Are there any further ties to be explored?

Mentis, A. A., Bougea, A. M., & Chrousos, G. P. (2021) · Aging Brain · doi:10.1016/j.nbas.2021.100024 · Cited by 20

The chloride antiporter CLCN7 is a modifier of lysosome dysfunction in FIG4 and VAC14 mutants

Cao, X., Lenk, G. M., Mikušević, V., Mindell, J. A., & Meisler, M. H. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010800 · Cited by 20

Phosphoinositides in Neuroexocytosis and Neuronal Diseases

Wen, P. J., Osborne, S. L., & Meunier, F. A. (2012) · Current topics in microbiology and immunology · doi:10.1007/978-94-007-5025-8_4 · Cited by 19

An Introduction to Phosphoinositides

Maffucci, T. (2012) · Current topics in microbiology and immunology · doi:10.1007/978-94-007-5025-8_1 · Cited by 19

PIKfyve Deficiency in Myeloid Cells Impairs Lysosomal Homeostasis in Macrophages and Promotes Systemic Inflammation in Mice

Min, S. H., Suzuki, A., Weaver, L. K., Guzman, J. F., Chung, Y., Jin, H., Santos, F. G. D. L., Trasorras, C., Zhao, L., Spruce, L. A., et al. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00158-19 · Cited by 17

The roles of phosphoinositides in mammalian autophagy

Jang, D., & Lee, J. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0777-x · Cited by 16

Cellular vacuolization caused by overexpression of the PIKfyve-binding deficient Vac14L156R is rescued by starvation and inhibition of vacuolar-ATPase

Schulze, U., Vollenbröker, B., Kühnl, A., Granado, D., Bayraktar, S., Rescher, U., Pavenstädt, H., & Weide, T. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.02.012 · Cited by 15

The role of autophagy in the pathogenesis and treatment of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)

Beckers, J., & Damme, P. V. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2474796 · Cited by 19

Autophagy contributes to lysosomal storage disorders

Shimada, Y., & Klionsky, D. (2012) · Autophagy · doi:10.4161/auto.19920 · Cited by 15

Condition-dependent functional shift of two Drosophila Mtmr lipid phosphatases in autophagy control

Manzéger, A., Tagscherer, K., Lőrincz, P., Szaker, H. M., Lukácsovich, T., Pilz, P., Kméczik, R., Csikós, G., Erdélyi, M., Sass, M., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1899681 · Cited by 15

The Interplay Between Autophagy and RNA Homeostasis: Implications for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Houghton, O. H., Mizielinska, S., & Gómez‐Suaga, P. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.838402 · Cited by 12

The Pathogenesis of Pancreatitis and the Role of Autophagy

Tsomidis, I., Voumvouraki, A., & Kouroumalis, E. (2024) · Gastroenterology Insights · doi:10.3390/gastroent15020022 · Cited by 14

The Lysosomal Storage Disorder Due to fig4a Mutation Causes Robust Liver Vacuolation in Zebrafish

Bao, W., Wang, X., Luo, L., & Ni, R. (2021) · Zebrafish · doi:10.1089/zeb.2020.1911 · Cited by 12

Distinct Requirements for Vacuolar Protein Sorting 34 Downstream Effector Phosphatidylinositol 3-Phosphate 5-Kinase in Podocytes Versus Proximal Tubular Cells

Venkatareddy, M. P., Verma, R. K., Kalinowski, A. H., Patel, S. R., Shisheva, A., & Garg, P. K. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015050555 · Cited by 12

Regulation of glial size by eicosapentaenoic acid through a novel Golgi apparatus mechanism

Zhang, A., Guan, Z., Ockerman, K. M., Dong, P., Guo, J., Wang, Z., & Yan, D. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3001051 · Cited by 12

C9ORF72-derived poly-GA DPRs undergo endocytic uptake in iAstrocytes and spread to motor neurons

Marchi, P. M., Marrone, L., Brasseur, L., Coens, A., Webster, C. P., Bousset, L., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202101276 · Cited by 17

FIG4 downregulation-arrested autophagy-lysosomal degradation of IL-18 drives lipid-associated macrophage polarization and immunotherapy resistance in triple-negative breast cancer

Xia, F., Zhu, X., Li, X., Yi, Q., Zhou, S., Wang, J., Wang, X., Zhang, K., Zhan, C., Tang, H., et al. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218278 · Cited by 10

Autophagy and Motor Neuron Diseases

Zhang, X., Yang, K., & Le, W. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-4272-5_3 · Cited by 9

Essential roles of phosphatidylinositol 4-phosphate phosphatases Sac1p and Sjl3p in yeast autophagosome formation

Muramoto, M., Yamakuchi, Y., Konishi, R., Koudatsu, S., Tomikura, H., Fukuda, K., Kuriyama, S., Kurokawa, Y., Masatani, T., Tamaki, H., et al. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2022.159184 · Cited by 7

The Protein Complex of Neurodegeneration-related Phosphoinositide Phosphatase Sac3 and ArPIKfyve Binds the Lewy Body-associated Synphilin-1, Preventing Its Aggregation

Ikonomov, O. C., Sbrissa, D., Compton, L. M., Kumar, R., Tisdale, E. J., Chen, X., & Shisheva, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.669929 · Cited by 8

Analysis, Regulation, and Roles of Endosomal Phosphoinositides

Maffucci, T., & Falasca, M. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-397925-4.00005-5 · Cited by 8

Roles of class III phosphatidylinositol 3-kinase, Vps34, in phagocytosis, autophagy, and endocytosis in retinal pigmented epithelium

He, F., Nichols, R. M., Agosto, M. A., & Wensel, T. G. (2025) · iScience · doi:10.1016/j.isci.2025.112371 · Cited by 7

Clinical Characteristics of Charcot-Marie-Tooth Disease Type 4J

Sadjadi, R., Picher‐Martel, V., Morrow, J. M., Thedens, D. R., DiCamillo, P. A., McCray, B. A., Pareyson, D., Herrmann, D. N., Reilly, M. M., Li, J., et al. (2024) · Neurology · doi:10.1212/wnl.0000000000209763 · Cited by 7

Proximity Interactome Map of the Vac14–Fig4 Complex Using BioID

Qiu, S., Lavallée‐Adam, M., & Côté, M. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00408 · Cited by 7

Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation

Yoo, K.-Y., Son, J. Y., Lee, J. U., Shin, W., Im, D.-W., Kim, S. J., Ryu, S. E., & Heo, Y.-S. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471500927x · Cited by 7

Emerging drug targets in amyotrophic lateral sclerosis

Bova, M. P., & Kinney, G. G. (2012) · Expert Opinion on Orphan Drugs · doi:10.1080/21678707.2013.744949 · Cited by 6

Murine Fig4 is dispensable for muscle development but required for muscle function

Reifler, A. N., Lenk, G. M., Li, X., Groom, L. A., Brooks, S. V., Wilson, D., Bowerson, M., Dirksen, R. T., Meisler, M. H., & Dowling, J. J. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-21 · Cited by 6

Loss-of-function mutation in Hippo suppressed enlargement of lysosomes and neurodegeneration caused by dFIG4 knockdown

Kushimura, Y., Azuma, Y., Mizuta, I., Muraoka, Y., Kyotani, A., Yoshida, H., Tokuda, T., Mizuno, T., & Yamaguchi, M. (2018) · Neuroreport · doi:10.1097/wnr.0000000000001044 · Cited by 6

Altered phenotypes due to genetic interaction between the mouse phosphoinositide biosynthesis genes Fig4 and Pip4k2c

Cao, X., Lenk, G. M., & Meisler, M. H. (2023) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkad007 · Cited by 5

Sequestosome 1/p62: a multi-domain protein with multi-faceted functions

Liu, X., Gál, J., & Zhu, H. (2012) · Frontiers in Biology · doi:10.1007/s11515-012-1217-z · Cited by 5

Phosphoinositide phosphatase Sac3 regulates the cell surface expression of scavenger receptor A and formation of lipid droplets in macrophages

Morioka, S., Nigorikawa, K., Hazeki, K., Ohmura, M., Sakamoto, H., Matsumura, T., Takasuga, S., & Hazeki, O. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.022 · Cited by 5

Vac14 protein multimerization is a prerequisite step for Fab1 protein complex assembly and function

Alghamdi, T. A., Ho, C. Y., Mrakovic, A., Taylor, D. L., Mao, D. Y. L., & Botelho, R. (2023) · doi:10.32920/21982883.v1 · Cited by 5

Lysosomal swelling triggers LRRK2 activityPreprint

Malankhanova, T., Liu, Z., Strader, S., Wang, W., Sung, K., Li, Z., Ferguson, S. M., & West, A. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.09.693280 · Cited by 4

Comparative Analysis of Two Autophagy-Enhancing Small Molecules (AUTEN-67 and -99) in a Drosophila Model of Spinocerebellar Ataxia Type 1

Burján, T., Aslam, M., Keresztes, F., Sigmond, T., Billes, V., Bencsik, N., Schlett, K., Vellai, T., & Kovács, A. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110443 · Cited by 3

Lysosome enlargement during inhibition of the lipid kinase PIKfyve proceeds through lysosome coalescence

Choy, C. H., Saffi, G. T., Gray, M. A., Wallace, C. T., Dayam, R. M., Ou, Z.-Y. A., Lenk, G. M., Puertollano, R., Watkins, S. C., & Botelho, R. (2023) · doi:10.32920/21982919 · Cited by 3

The vacuolar morphology protein VAC14 plays an important role in sexual development in the filamentous ascomycete Sordaria macrospora

Groth, A., Ahlmann, S., Werner, A., & Pöggeler, S. (2022) · Current Genetics · doi:10.1007/s00294-022-01244-0 · Cited by 2

Lipid Metabolism: Key Determinant in Neurodegenerative Diseases

Yadav, M., Gupta, J., & Agrawal, N. (2024) · Springer eBooks · doi:10.1007/978-981-97-4288-2_6 · Cited by 2

Lipid Codes and Lipid‐Binding Proteins as Central Regulators of Autophagy

Kumar, A., & Ghosh, D. K. (2026) · BioFactors · doi:10.1002/biof.70124 · Cited by 1

Role of Phosphoinositides in Membrane Traffic

Sheffield, D. A., Gurung, R., & Mitchell, C. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.20051-5 · Cited by 1

The interplay between Lewy body-like alpha-synuclein aggregates and protein degradation pathways in a cell-based model of Parkinson's disease

Tanik, S. A. (2013) · Scholarly Commons (University of Pennsylvania) · Cited by 1

DRAM1 requires PI(3,5)P 2 generation by PIKfyve to deliver vesicles and their cargo to endolysosomesPreprint

van der Vaart, M., Banducci-Karp, A., Forn‐Cuní, G., Witt, P. M. M., Willemse, J. J., Muñoz‐Sánchez, S., Hosseini, R., & Meijer, A. H. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.15.422832 · Cited by 1

Early responses to hyperosmotic stress at the yeast vacuolePreprint

Saravanan, K., & Kane, P. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.11.669746 · Cited by 1

Structural, biochemical, and cell biological characterization of RAB7 mutants that cause peripheral neuropathy

McCray, B. A. (2010) · ScholarlyCommons (University of Pennsylvania)

Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3

Son, J. Y., Lee, J. U., Yoo, K.-Y., Shin, W., Im, D.-W., Kim, S. J., Ryu, S. E., & Heo, Y. (2014) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x14015714

Regulation of TRPML1 by Lipids in Lysosomes.

Shen, D. (2012) · Deep Blue (University of Michigan)

Structural and functional characterization of interactions of myotubularin-related proteins

Gegenschatz‐Schmid, K. (2012) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-007313479

Peripheral Nerve Neuropathies Including Charcot–Marie–Tooth Disease

Pandraud, A., & Houlden, H. (2017) · Neurodegeneration · doi:10.1002/9781118661895.ch19

Familial Amyotrophic Lateral Sclerosis with a focus on C9orf72 Hexanucleotide GGGGCC Repeat Expansion Associated ALS with Frontotemporal Dementia

Workinger, P. M. (2017) · UA Campus Repository (The University of Arizona)

Autophagy Is Up Regulated In A Neuronal Model Of Charcot-Marie Tooth Disease That Overexpresses Dynamin 2 Mutant

(2017) · International Journal of Neuroscience Research · doi:10.28933/ijnr-2017-03-2801

Mitochondrial-localized Phosphatidylethanolamine in Mitochondrial Dynamics and Autophagy

Chan, E. Y. L. (2014) · TSpace (University of Toronto)

Signalling from Endosomes in Neurodevelopment and Neurodegenerative Disorders

Markworth, R. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8920

Faculty Opinions recommendation of PIKfyve regulates melanosome biogenesis.

Fukuda, M., & Ohbayashi, N. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732916084.793574984

Characterizing the VAC14 multimeric state

Ho, S. C. Y. (2021) · doi:10.32920/ryerson.14655660.v1

Regulation of lysosome biogenesis by phosphoinositides and phagocytosis

Choy, C. (2021) · doi:10.32920/ryerson.14648823.v1

Characterizing the VAC14 multimeric state

Ho, S. C. Y. (2021) · doi:10.32920/ryerson.14655660

Role of Phosphoinositides in Membrane Traffic

Sheffield, D. A., Gurung, R., & Mitchell, C. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.20051-5

Lysosome enlargement during inhibition of the lipid kinase PIKfyve proceeds through lysosome coalescence

Choy, C. H., Saffi, G. T., Gray, M. A., Wallace, C. T., Dayam, R. M., Ou, Z.-Y. A., Lenk, G. M., Puertollano, R., Watkins, S. C., & Botelho, R. (2023) · doi:10.32920/21982919.v1

Vac14 protein multimerization is a prerequisite step for Fab1 protein complex assembly and function

Alghamdi, T. A., Ho, C. Y., Mrakovic, A., Taylor, D. L., Mao, D. Y. L., & Botelho, R. (2023) · doi:10.32920/21982883

Understanding the Regulation of TFEB and Rab7 and Their Contributions to Lysosomal Adaptation

Alves, P. (2023) · doi:10.32920/24076293.v1

Stressz-indukált autofágia szabályozási mechanizmusai Drosophila melanogasterben

Manzéger, A. (2023) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2022.245

Échapper à la mort cellulaire dans le cancer : mitophagie et régulation de la mort indépendante des caspases

Villa, E. (2017) · theses.fr (ABES) · doi:10.70675/f0d1579dzdd47z4ac8z82abz4e3b85a0100b

Signalisation et implication des phosphoinositides dans la myopathie myotubulaire liée à l'X

Mansat, M. (2022) · theses.fr (ABES) · doi:10.70675/ff8ec5a0z1358z4abdzac6az4cc19fb4f41e

PIKfyve mediates the maturation of mycobacteria-containing vesicles

Muñoz‐Sánchez, S., van der Vaart, M., & Meijer, A. H. (2026) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2026.1792069

Early-onset neuroinflammation drives neurodegeneration caused by lysosomal PI(3,5)P2 insufficiency

Wong, B., Payne, M., Silva, A., Kurniawan, E., Eidman, A. S., Pizzo, D. P., Rajupalem, R., Lenk, G. M., Paulo, J. A., Khan, T., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107467

Dysregulated PIKfyve-dependent inhibition of ClC-7 causes ammonium-dependent endolysosomal vacuolization and autophagic flux impairment: Rescue by glutaminase inhibition

Uwada, J., Nakazawa, H., Yazawa, T., Muramatsu, I., & Masuoka, T. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2026.120239

Autophagy and cell-autonomy in mouse models of PI(3, 5)P2 deficiency

Ferguson, C. (2011) · Deep Blue (University of Michigan)

PtdIns(3,5)P2and autophagy in mouse models of neurodegeneration

Ferguson, C., Lenk, G. M., & Meisler, M. H. (2010) · Autophagy · doi:10.4161/auto.6.1.10626 · Cited by 32

Mouse Models of PI(3,5)P2 Deficiency with Impaired Lysosome Function

Lenk, G. M., & Meisler, M. H. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-397926-1.00014-7 · Cited by 40

Early-onset neuroinflammation drives neurodegeneration caused by lysosomal PI(3,5)P2 insufficiency

Wong, B., Payne, M., Silva, A., Kurniawan, E., Eidman, A. S., Pizzo, D. P., Rajupalem, R., Lenk, G. M., Paulo, J. A., Khan, T., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107467

Mutations in PI(3,5)P2 Signaling and Neurodegeneration in Mouse and Human.

Chow, C. Y. (2008) · Deep Blue (University of Michigan)