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Physiological and pathological functions of TMEM106B: a gene associated with brain aging and multiple brain disorders
Open accessAbstract
TMEM106B, encoding a lysosome membrane protein, has been recently associated with brain aging, hypomyelinating leukodystrophy and multiple neurodegenerative diseases, such as frontotemporal lobar degeneration (FTLD) and limbic-predominant age-related TDP-43 encephalopathy (LATE). During the past decade, considerable progress has been made towards our understanding of the cellular and physiological functions of TMEM106B. TMEM106B regulates many aspects of lysosomal function, including lysosomal pH, lysosome movement, and lysosome exocytosis. Both an increase and decrease in TMEM106B levels result in lysosomal abnormalities. In mouse models, TMEM106B deficiency leads to lysosome trafficking and myelination defects and FTLD related pathology. In humans, alterations in TMEM106B levels or function are intimately linked to neuronal proportions, brain aging, and brain disorders. Further elucidation of the physiological function of TMEM106B and changes in TMEM106B under pathological conditions will facilitate therapeutic development to treat brain disorders associated with TMEM106B.
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“Interestingly, both GRN and TMEM106B are reported to be involved in defective endosome/lysosome trafficking/function49,50, a defect that is also observed in AD.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [50]
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“we examined TMEM106B 101-103 and necroptosis effector MLKL 104,105 (Fig. 5c-d), two molecules previously implicated in neurodegeneration of AD, and detected no significant changes.”
From NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease (2025) · cites this paper as [103]
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Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
TFEB Links Autophagy to Lysosomal Biogenesis
Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365
Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058
Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis
Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 1×
“FTLD overlaps in pathology and genetic causes with amyotrophic lateral sclerosis (ALS), and these two are often considered part of a continuous disease spectrum [45].”
BackgroundState of play in amyotrophic lateral sclerosis genetics
Renton, A. E., Chiò, A., & Traynor, B. J. (2013) · Nature Neuroscience · doi:10.1038/nn.3584 · Cited by 1,626
Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report
Nelson, P. T., Dickson, D. W., Trojanowski, J. Q., Jack, C. R., Boyle, P. A., Arfanakis, K., Rademakers, R., Alafuzoff, I., Attems, J., Brayne, C., et al. (2019) · Brain · doi:10.1093/brain/awz099 · Cited by 1,547
Autophagy pathway: Cellular and molecular mechanisms
Yu, L., Chen, Y., & Tooze, S. A. (2017) · Autophagy · doi:10.1080/15548627.2017.1378838 · Cited by 1,522
Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512
The prevalence of frontotemporal dementia
Ratnavalli, E., Brayne, C., Dawson, K. E., & Hodges, J. R. (2002) · Neurology · doi:10.1212/wnl.58.11.1615 · Cited by 1,182
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134
Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration
Gass, J. M., Cannon, A. D., Mackenzie, I. R., Boeve, B. F., Baker, M. C., Adamson, J. L., Crook, R., Melquist, S., Kuntz, K., Petersen, R. C., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl241 · Cited by 587
Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions
Van Deerlin, V. M., Sleiman, P. M. A., Martinez-Lage, M., Chen-Plotkin, A., Wang, L.-S., Graff-Radford, N. R., Dickson, D. W., Rademakers, R., Boeve, B. F., Grossman, M., et al. (2010) · Nature Genetics · doi:10.1038/ng.536 · Cited by 579
Mechanisms and functions of lysosome positioning
Pu, J., Guardia, C. M., Keren-Kaplan, T., & Bonifacino, J. S. (2016) · Journal of Cell Science · doi:10.1242/jcs.196287 · Cited by 570
Neary, D., Snowden, J. S., & Mann, D. M. A. (2005) · The Lancet Neurology · doi:10.1016/s1474-4422(05)70223-4 · Cited by 558
TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets
Scotter, E. L., Chen, H.-J., & Shaw, C. E. (2015) · Neurotherapeutics · doi:10.1007/s13311-015-0338-x · Cited by 382
The granulin gene family: from cancer to dementia
Bateman, A., & Bennett, H. P. J. (2009) · BioEssays · doi:10.1002/bies.200900086 · Cited by 340
Chronic traumatic encephalopathy pathology in a neurodegenerative disorders brain bank
Bieniek, K. F., Ross, O. A., Cormier, K. A., Walton, R. L., Soto-Ortolaza, A., Johnston, A. E., DeSaro, P., Boylan, K. B., Graff-Radford, N. R., Wszolek, Z. K., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1502-4 · Cited by 323
Lysosomal Biology and Function: Modern View of Cellular Debris Bin
Trivedi, P. C., Bartlett, J. J., & Pulinilkunnil, T. (2020) · Cells · doi:10.3390/cells9051131 · Cited by 309
A novel Alzheimer disease locus located near the gene encoding tau protein
Jun, G., Ibrahim-Verbaas, C. A., Vronskaya, M., Lambert, J.-C., Chung, J., Naj, A. C., Kunkle, B. W., Wang, L.-S., Bis, J. C., Bellenguez, C., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2015.23 · Cited by 297
Lysosome trafficking and signaling in health and neurodegenerative diseases
Lie, P. P. Y., & Nixon, R. A. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.015 · Cited by 277
TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
Cohen, T. J., Lee, V. M. ‐., & Trojanowski, J. Q. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.06.004 · Cited by 271
Thompson, J. C., Stopford, C. L., Snowden, J., & Neary, D. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2003.033779 · Cited by 267
Moving and positioning the endolysosomal system
Bonifacino, J. S., & Neefjes, J. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.01.008 · Cited by 253
Progranulin, lysosomal regulation and neurodegenerative disease
Kao, A. W., McKay, A. S., Singh, P. P., Brunet, A., & Huang, E. J. (2017) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.36 · Cited by 252
TMEM106B regulates progranulin levels and the penetrance of FTLD in GRN mutation carriers
Finch, N., Carrasquillo, M. M., Baker, M., Rutherford, N. J., Coppola, G., DeJesus-Hernandez, M., Crook, R., Hunter, T., Ghidoni, R., Benussi, L., et al. (2011) · Neurology · doi:10.1212/wnl.0b013e31820a0e3b · Cited by 243
Cenik, B., Sephton, C. F., Cenik, B. K., Herz, J., & Yu, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.399170 · Cited by 235
Neuron-glia communication in the control of oligodendrocyte function and myelin biogenesis
Simons, M., & Trajković, K. (2006) · Journal of Cell Science · doi:10.1242/jcs.03242 · Cited by 233
Pathomechanisms of TDP‐43 in neurodegeneration
Gao, J., Wang, L., Huntley, M. L., Perry, G. L., & Wang, X. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14327 · Cited by 232
Chen-Plotkin, A. S., Unger, T. L., Gallagher, M. D., Bill, E., Kwong, L. K., Volpicelli-Daley, L., Busch, J. I., Akle, S., Grossman, M., Van Deerlin, V., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0521-12.2012 · Cited by 230
The lysosomal function of progranulin, a guardian against neurodegeneration
Paushter, D. H., Du, H., Feng, T., & Hu, F. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1861-8 · Cited by 230
Self-citationde Araújo, M. E. G., Liebscher, G., Hess, M. W., & Huber, L. A. (2019) · Traffic · doi:10.1111/tra.12714 · Cited by 210
Brady, O. A., Zheng, Y., Murphy, K. A., Huang, M. J., & Hu, F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds475 · Cited by 205
Self-citationGötzl, J. K., Mori, K., Daμμe, M., Fellerer, K., Tahirović, S., Kleinberger, G., Janssens, J., van der Zee, J., Lang, C. M., Kremmer, E., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1262-6 · Cited by 196
Cruchaga, C., Graff, C., Chiang, H., Wang, J., Hinrichs, A. L., Spiegel, N., Bertelsen, S. E., Mayo, K., Norton, J. B., Morris, J. C., et al. (2011) · Archives of Neurology · doi:10.1001/archneurol.2010.350 · Cited by 189
The FTLD risk factor TMEM106B and MAP6 control dendritic trafficking of lysosomes
Schwenk, B. M., Lang, C. M., Hogl, S., Tahirović, S., Orozco, D., Rentzsch, K., Lichtenthaler, S. F., Hoogenraad, C. C., Capell, A., Haass, C., et al. (2013) · The EMBO Journal · doi:10.1002/embj.201385857 · Cited by 168
Lang, C. M., Fellerer, K., Schwenk, B. M., Kuhn, P., Kremmer, E., Edbauer, D., Capell, A., & Haass, C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.365098 · Cited by 165
Yang, G., Yuan, Y., Yuan, H., Wang, J., Yun, H., Geng, Y., Zhao, M., Li, L., Weng, Y., Liu, Z., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050967 · Cited by 165
Klein, Z. A., Takahashi, H., Ma, M., Stagi, M., Zhou, M. S., Lam, T. T., & Strittmatter, S. M. (2017) · Neuron · doi:10.1016/j.neuron.2017.06.026 · Cited by 162
TMEM106B protects C9ORF72 expansion carriers against frontotemporal dementia
van Blitterswijk, M., Mullen, B., Nicholson, A. M., Bieniek, K. F., Heckman, M. G., Baker, M., DeJesus‐Hernandez, M., Finch, N. A., Brown, P. H., Murray, M. E., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1240-4 · Cited by 154
Gallagher, M. D., Suh, E. R., Grossman, M., Elman, L. B., McCluskey, L. F., Swieten, J. C. V., Al‐Sarraj, S., Neumann, M., Gelpí, E., Ghetti, B. F., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1239-x · Cited by 148
How Lysosomes Sense, Integrate, and Cope with Stress
Säftig, P., & Puertollano, R. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.09.004 · Cited by 139
Lysosome size, motility and stress response regulated by fronto-temporal dementia modifier TMEM106B
Stagi, M., Klein, Z. A., Gould, T. J., Bewersdorf, J., & Strittmatter, S. M. (2014) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.07.006 · Cited by 137
Holler, C. J., Taylor, G., Deng, Q., & Kukar, T. L. (2017) · eNeuro · doi:10.1523/eneuro.0100-17.2017 · Cited by 137
Pottier, C., Zhou, X., Perkerson, R. B., Baker, M., Jenkins, G. D., Serie, D. J., Ghidoni, R., Benussi, L., Binetti, G., López de Munain, A., et al. (2018) · The Lancet Neurology · doi:10.1016/s1474-4422(18)30126-1 · Cited by 131
Rhinn, H., & Abeliovich, A. (2017) · Cell Systems · doi:10.1016/j.cels.2017.02.009 · Cited by 130
Gamp, A.-C., Tanaka, Y., Lüllmann-Rauch, R., Wittke, D., D’Hooge, R., Deyn, P. P. D., Moser, T., Maier, H., Hartmann, D., Reiss, K., et al. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg062 · Cited by 127
van der Zee, J., Langenhove, T. V., Kleinberger, G., Sleegers, K., Engelborghs, S., Vandenberghe, R. R., Santens, P., den Broeck, M. V., Joris, G., Brys, J., et al. (2011) · Brain · doi:10.1093/brain/awr007 · Cited by 127
TMEM 106B p.T185S regulates TMEM 106B protein levels: implications for frontotemporal dementia
Nicholson, A. M., Finch, N. A., Wojtas, A., Baker, M. C., Perkerson, R. B., Castanedes‐Casey, M., Rousseau, L., Benussi, L., Binetti, G. G., Ghidoni, R., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12329 · Cited by 124
Kundu, S. T., Grzeskowiak, C. L., Fradette, J. J., Gibson, L. A., Rodriguez, L. B., Creighton, C. J., Scott, K. L., & Gibbons, D. L. (2018) · Nature Communications · doi:10.1038/s41467-018-05013-x · Cited by 124
Risk genotypes at TMEM106B are associated with cognitive impairment in amyotrophic lateral sclerosis
Vass, R., Ashbridge, E., Geser, F., Hu, W. T., Grossman, M., Clay-Falcone, D., Elman, L., McCluskey, L., Lee, V. M. Y., Van Deerlin, V. M., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0782-y · Cited by 119
Gao, K., Pi, Y., Mu, C., Peng, Y., Huang, Z., & Zhu, W. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14333 · Cited by 119
A Dementia-Associated Risk Variant near TMEM106B Alters Chromatin Architecture and Gene Expression
Gallagher, M. D., Posavi, M., Huang, P., Unger, T. L., Berlyand, Y., Gruenewald, A. L., Chesi, A., Manduchi, E., Wells, A. D., Grant, S. F. A., et al. (2017) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2017.09.004 · Cited by 112
White, C. C., Yang, H., Yu, L., Chibnik, L. B., Dawe, R. J., Yang, J., Klein, H., Felsky, D., Ramos‐Miguel, A., Arfanakis, K., et al. (2017) · PLoS Medicine · doi:10.1371/journal.pmed.1002287 · Cited by 105
TMEM106B risk variant is implicated in the pathologic presentation of Alzheimer disease
Rutherford, N. J., Carrasquillo, M. M., Li, M., Bisceglio, G. D., Menke, J. R., Josephs, K. A., Parisi, J. E., Petersen, R. C., Graff‐Radford, N. R., Younkin, S. G., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e318264e3ac · Cited by 97
Loss of TMEM106B and PGRN leads to severe lysosomal abnormalities and neurodegeneration in mice
Feng, T., Mai, S., Roscoe, J. M., Sheng, R. R., Ullah, M., Zhang, J., Katz, I. I., Yu, H., Xiong, W., & Hu, F. (2020) · The EMBO Reports · doi:10.15252/embr.202050219 · Cited by 94
Self-citationDistinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling
Winterstein, C., Trotter, J., & Krämer-Albers, E.-M. (2008) · Journal of Cell Science · doi:10.1242/jcs.022731 · Cited by 92
The TMEM106B locus and TDP-43 pathology in older persons without FTLD
Yu, L., Jager, P. L. D., Yang, J., Trojanowski, J. Q., Bennett, D. A., & Schneider, J. A. (2015) · Neurology · doi:10.1212/wnl.0000000000001313 · Cited by 91
Biology and Pathobiology of TDP-43 and Emergent Therapeutic StrategiesPreprint
Guo, L. E., & Shorter, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024554 · Cited by 85
Li, Z., Farias, F. H. G., Dube, U., Del-Aguila, J. L., Mihindukulasuriya, K. A., Fernandez, M. V., Ibanez, L., Budde, J. P., Wang, F., Lake, A. M., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02066-0 · Cited by 85
A recurrent de novo mutation in TMEM106B causes hypomyelinating leukodystrophy
Simons, C., Dyment, D. A., Bent, S. J., Crawford, J., D’Hooghe, M., Kohlschütter, A., Venkateswaran, S., Helman, G., Poll‐The, B. T., Makowski, C. C., et al. (2017) · Brain · doi:10.1093/brain/awx314 · Cited by 83
TMEM106B Effect on cognition in Parkinson disease and frontotemporal dementia
Tropea, T. F., Mak, J., Guo, M. H., Xie, S. X., Suh, E., Rick, J., Siderowf, A., Weintraub, D., Grossman, M., Irwin, D., et al. (2019) · Annals of Neurology · doi:10.1002/ana.25486 · Cited by 83
The Lysosomal Sialic Acid Transporter Sialin Is Required for Normal CNS Myelination
Prolo, L. M., Vogel, H. S., & Reimer, R. J. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3005-09.2009 · Cited by 76
Lüningschrör, P., Werner, G., Stroobants, S., Kakuta, S., Dombert, B., Sinske, D., Wanner, R., Lüllmann-rauch, R., Wefers, B., Wurst, W., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.060 · Cited by 75
Loss of TMEM106B potentiates lysosomal and FTLD‐like pathology in progranulin‐deficient mice
Werner, G., Daμμe, M., Schludi, M. H., Gnörich, J. S., Wind-Mark, K., Fellerer, K., Wefers, B., Wurst, W., Edbauer, D., Brendel, M., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050241 · Cited by 75
Nelson, P. T., Wang, W., Partch, A. B., Monsell, S. E., Valladares, O., Ellingson, S. R., Wilfred, B. R., Naj, A. C., Wang, L.-S., Kukull, W. A., et al. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000151 · Cited by 69
Variation in TMEM106B in chronic traumatic encephalopathy
Cherry, J. D., Mez, J., Crary, J. F., Tripodis, Y., Alvarez, V. E., Mahar, I., Huber, B. R., Alosco, M. L., Nicks, R., Abdolmohammadi, B., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0619-9 · Cited by 67
Zhou, X., Nicholson, A. M., Ren, Y., Brooks, M., Jiang, P., Zuberi, A. R., Phuoc, H. N., Perkerson, R. B., Matchett, B. J., Parsons, T. M., et al. (2020) · Brain · doi:10.1093/brain/awaa141 · Cited by 66
Zhou, X., Brooks, M., Jiang, P., Koga, S., Zuberi, A. R., Baker, M., Parsons, T. M., Castanedes‐Casey, M., Phillips, V. R., Librero, A. L., et al. (2020) · EMBO Reports · doi:10.15252/embr.202050197 · Cited by 64
Koga, S., Lin, W. ‐., Walton, R. L., Ross, O. A., & Dickson, D. W. (2018) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12485 · Cited by 57
A role of the frontotemporal lobar degeneration risk factor TMEM106B in myelination
Feng, T., Sheng, R. R., Solé‐Domènech, S., Ullah, M., Zhou, X., Mendoza, C. S., Enriquez, L. C. M., Katz, I. I., Paushter, D. H., Sullivan, P. M., et al. (2020) · Brain · doi:10.1093/brain/awaa154 · Cited by 53
Self-citationMilind, N., Preuß, C., Haber, A., Ananda, G., Mukherjee, S., Cai, J., Shapley, S. M., Tyler, A. L., Logsdon, B. A., Crane, P. K., et al. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008775 · Cited by 51
Schmiedt, M.-L., Blom, T., Blom, T., Kopra, O., Wong, A. P., von Schantz, C., Ikonen, E., Kuronen, M., Jauhiainen, M., Cooper, J. D., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.009 · Cited by 49
TDP-43 in neurodegenerative disorders
Cook, C. N., Zhang, Y., Xu, Y.-F., Dickson, D. W., & Petrucelli, L. (2008) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.8.7.969 · Cited by 49
Zhou, X., Sun, L., Brady, O. A., Murphy, K. A., & Hu, F. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0412-1 · Cited by 49
Self-citationBrady, O. A., Zhou, X., & Hu, F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515700 · Cited by 48
Self-citationTMEM106B haplotypes have distinct gene expression patterns in aged brain
Ren, Y., van Blitterswijk, M., Allen, M., Carrasquillo, M. M., Reddy, J. S., Wang, X., Beach, T. G., Dickson, D. W., Ertekin‐Taner, N., Asmann, Y. W., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0268-2 · Cited by 47
Genetics of Gene Expression in the Aging Human Brain Reveal TDP-43 Proteinopathy Pathophysiology
Yang, H.-S., White, C. C., Klein, H.-U., Yu, L., Gaiteri, C., Ma, Y., Felsky, D., Mostafavi, S., Petyuk, V. A., Sperling, R. A., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.05.010 · Cited by 47
Lattante, S., Ber, I. L., Galimberti, D., Serpente, M., Rivaud-Péchoux, S., Camuzat, A., Clot, F., Fenoglio, C., Scarpini, E. A., Brice, A., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.06.023 · Cited by 44
Jun, M.-H., Han, J. H., Lee, Y.-K., Jang, D., Kaang, B., & Lee, J. (2015) · Molecular Brain · doi:10.1186/s13041-015-0177-z · Cited by 38
Partial Tmem106b reduction does not correct abnormalities due to progranulin haploinsufficiency
Arrant, A. E., Nicholson, A. M., Zhou, X., Rademakers, R., & Roberson, E. D. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0264-6 · Cited by 36
Hokkanen, S. R. K., Kero, M., Kaivola, K., Hunter, S., Keage, H. A. D., Kiviharju, A., Raunio, A., Tienari, P. J., Paetau, A. E., Matthews, F. E., et al. (2019) · Brain Pathology · doi:10.1111/bpa.12773 · Cited by 34
Adams, H. H. H., Verhaaren, B. F. J., Vrooman, H. A., Uitterlinden, A. G., Albert Hofman, D., van Duijn, C. M., van der Lugt, A., Niessen, W. J., Vernooij, M. W., & Ikram, M. A. (2014) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.03.006 · Cited by 31
Stroobants, S., D’Hooge, R., & Daμμe, M. (2020) · Brain Pathology · doi:10.1111/bpa.12903 · Cited by 31
Yan, H., Kubisiak, T. L., Ji, H., Xiao, J., Wang, J., & Burmeister, M. (2018) · Brain · doi:10.1093/brain/awy029 · Cited by 29
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Metadata
- Authors
- Feng, T., Lacrampe, A., & Hu, F.
- Affiliations
- Cornell University (US)
- Corresponding author
- Hu, Fenghua
- Venue
- Acta Neuropathologica
- Published
- 2021-01-01
- Volume
- 141
- Issue
- 3
- Pages
- 327-339
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC8049516
- OpenAlex
- W3114567345
- Cited by
- 110
- References
- 94
- Citations by year
- 2026: 13 · 2025: 27 · 2024: 25 · 2023: 25 · 2022: 13 · 2021: 6
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS088448 & R01NS095954)
- the Bluefield project to cure frontotemporal dementia
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- TMEM106B, lysosomal function, lysosomal pH, lysosomal trafficking, lysosome exocytosis, hypomyelinating leukodystrophy, frontotemporal lobar degeneration, limbic-predominant age-related TDP-43 encephalopathy, brain aging, myelination defects, neurodegenerative diseases
- MeSH terms
- Aging, Animals, Brain, Brain Diseases, Humans, Membrane Proteins, Nerve Tissue Proteins
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