CoChat
Sign Up
Cited by 15Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsMicrotubule and mitosis dynamics

Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS

Open access
Kanaan, Nicholas M.·2024·Cytoskeleton
DOI 10.1002/cm.21820PMC PMC10851165
Open this paper in CoChat — free accountOpen PDF

Abstract

The microtubule‐associated protein tau has gained significant attention over the last several decades primarily due to its apparent role in the pathogenesis of several diseases, most notably Alzheimer's disease. While the field has focused largely on tau's potential contributions to disease mechanisms, comparably less work has focused on normal tau physiology. Moreover, as the field has grown, some misconceptions and dogmas regarding normal tau physiology have become engrained in the traditional narrative. Here, one of the most common misconceptions regarding tau, namely its normal cellular/subcellular distribution in the CNS, is discussed. The literature describing the presence of tau in neuronal somata, dendrites, axons and synapses, as well as in glial cells is described. The origins for the erroneous description of tau as an “axon‐specific,” “axon‐enriched” and/or “neuron‐specific” protein are discussed as well. The goal of this work is to help address these specific dogmatic misconceptions and provide a concise description of tau's normal cellular/subcellular localization in the adult CNS. This information can help refine our collective understanding of‐ and hypotheses about tau biology and pathobiology.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1002/cm.21820

Cites

10 of 10 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 75

  1. Bachmann, S., Bell, M., Klimek, J., & Zempel, H. (2021). Differential effects of the six human TAU isoforms: Somatic retention of 2N-TAU and increased microtubule number induced by 4R-TAU. Frontiers in Neuro- science, 15, 643115. https://doi.org/10.3389/fnins.2021.643115 · DOI
  2. Balaji, V., Kaniyappan, S., Mandelkow, E., Wang, Y., & Mandelkow, E. M. (2018). Pathological missorting of endogenous MAPT/tau in neurons caused by failure of protein degradation systems. Autophagy, 14(12), 2139-2154. https://doi.org/10.1080/15548627.2018.1509607 · DOI
  3. Belkadi, A., & LoPresti, P. (2008). Truncated tau with the Fyn-binding domain and without the microtubule-binding domain hinders the mye- linating capacity of an oligodendrocyte cell line. Journal of Neurochem- istry, 107(2), 351-360. https://doi.org/10.1111/j.1471-4159.2008. 05600.x · DOI
  4. Bell, M., Bachmann, S., Klimek, J., Langerscheidt, F., & Zempel, H. (2021). Axonal TAU sorting requires the C-terminus of TAU but is indepen- dent of ANKG and TRIM46 enrichment at the AIS. Neuroscience, 461, 155-171. https://doi.org/10.1016/j.neuroscience.2021.01.041 · DOI
  5. Bell, M., & Zempel, H. (2022). A simple human cell model for TAU traffick- ing and tauopathy-related TAU pathology. Neural Regeneration Research, 17(4), 770-772. https://doi.org/10.4103/1673-5374. 322450 · DOI
  6. Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2023). Laser- induced axotomy of human iPSC-derived and murine primary neurons decreases somatic tau and AT8 tau phosphorylation: A single-cell approach to study effects of acute axonal damage. Cellular and Molecu- lar Neurobiology, 43(7), 3497-3510. https://doi.org/10.1007/s10571- 023-01359-z · DOI
  7. Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985). The distribution of tau in the mammalian central nervous system. The Journal of Cell Biology, 101(4), 1371-1378.
  8. Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1986). Differential localization of MAP-2 and tau in mammalian neurons in situ. Annals of the New York Academy of Sciences, 466, 145-166.
  9. Black, M. M., Slaughter, T., Moshiach, S., Obrocka, M., & Fischer, I. (1996). Tau is enriched on dynamic microtubules in the distal region of grow- ing axons. The Journal of Neuroscience, 16(11), 3601-3619. https://doi. org/10.1523/jneurosci.16-11-03601.1996 · DOI · Paper page
  10. Boyne, L. J., Tessler, A., Murray, M., & Fischer, I. (1995). Distribution of big tau in the central nervous system of the adult and developing rat. The Journal of Comparative Neurology, 358(2), 279-293. https://doi.org/ 10.1002/cne.903580209 · DOI
  11. Brady, R. M., Zinkowski, R. P., & Binder, L. I. (1995). Presence of tau in iso- lated nuclei from human brain. Neurobiology of Aging, 16(3), 479-486.
  12. Brandt, R., Leger, J., & Lee, G. (1995). Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. The Journal of Cell Biology, 131(5), 1327-1340.
  13. Brion, J. P., van den Bosch de Aguilar, P., & Flament-Durand, J. (1985). Senile dementia of the Alzheimer type: Morphological and immunocy- tochemical studies. In J. Traber & W. H. Gipsen (Eds.), Senile dementia of the Alzheimer type: Early diagnosis, neuropathology and animal models (Vol. 2, pp. 164-174). Springer-Verlag.
  14. Bullmann, T., Holzer, M., Mori, H., & Arendt, T. (2009). Pattern of tau iso- forms expression during development in vivo. International Journal of Developmental Neuroscience, 27(6), 591-597. https://doi.org/10. 1016/j.ijdevneu.2009.06.001 · DOI
  15. Busciglio, J., Ferreira, A., Steward, O., & Cáceres, A. (1987). An immunocy- tochemical and biochemical study of the microtubule-associated pro- tein tau during post-lesion afferent reorganization in the hippocampus of adult rats. Brain Research, 419(1-2), 244-252. https://doi.org/10. 1016/0006-8993(87)90590-7 · DOI
  16. Camero, S., Benítez, M. J., Barrantes, A., Ayuso, J. M., Cuadros, R., Avila, J., & Jiménez, J. S. (2014). Tau protein provides DNA with ther- modynamic and structural features which are similar to those found in histone-DNA complex. Journal of Alzheimer's Disease, 39(3), 649-660. https://doi.org/10.3233/jad-131415 · DOI
  17. Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977a). Physical and chemical properties of purified tau factor and the role of tau in micro- tubule assembly. Journal of Molecular Biology, 116(2), 227-247.
  18. Combs, B., Mueller, R. L., Morfini, G., Brady, S. T., & Kanaan, N. M. (2019). Tau and axonal transport misregulation in tauopathies. Advances in Experimental Medicine and Biology, 1184, 81-95. https://doi.org/10. 1007/978-981-32-9358-8_7 · DOI
  19. Dabir, D. V., Robinson, M. B., Swanson, E., Zhang, B., Trojanowski, J. Q., Lee, V. M., & Forman, M. S. (2006). Impaired glutamate transport in a mouse model of tau pathology in astrocytes. The Journal of Neurosci- ence, 26(2), 644-654. https://doi.org/10.1523/JNEUROSCI.3861- 1505.2006 · DOI
  20. Dotti, C. G., Banker, G. A., & Binder, L. I. (1987). The expression and distri- bution of the microtubule-associated proteins tau and microtubule- associated protein 2 in hippocampal neurons in the rat in situ and in cell culture. Neuroscience, 23(1), 121-130.
  21. Ezerskiy, L. A., Schoch, K. M., Sato, C., Beltcheva, M., Horie, K., Rigo, F., Martynowicz, R., Karch, C. M., Bateman, R. J., & Miller, T. M. (2022). Astrocytic 4R tau expression drives astrocyte reactivity and dysfunc- tion. JCI Insight, 7(1), e152012. https://doi.org/10.1172/jci.insight. 152012 · DOI
  22. Ferreira, A., Busciglio, J., & Cáceres, A. (1987). An immunocytochemical analysis of the ontogeny of the microtubule-associated proteins MAP-2 and tau in the nervous system of the rat. Brain Research, 431(1), 9-31. https://doi.org/10.1016/0165-3806(87)90191-x · DOI
  23. Fischer, I. (2022). Evolutionary perspective of big tau structure: 4a exon variants of MAPT. Frontiers in Molecular Neuroscience, 15, 1019999. https://doi.org/10.3389/fnmol.2022.1019999 · DOI
  24. Fischer, I. (2024). Big tau: What, how, where and why. Cytoskeleton, 81(1), 7-12. https://doi.org/10.1002/cm.21772 · DOI
  25. Fischer, I., & Baas, P. W. (2020). Resurrecting the mysteries of big tau. Trends in Neurosciences, 43(7), 493-504. https://doi.org/10.1016/j. tins.2020.04.007 · DOI
  26. Forman, M. S., Lal, D., Zhang, B., Dabir, D. V., Swanson, E., Lee, V. M., & Trojanowski, J. Q. (2005). Transgenic mouse model of tau pathology in astrocytes leading to nervous system degeneration. The Journal of Neuroscience, 25(14), 3539-3550. https://doi.org/10.1523/ JNEUROSCI.0081-05.2005 · DOI · Paper page
  27. Gartner, U., Janke, C., Holzer, M., Vanmechelen, E., & Arendt, T. (1998). Postmortem changes in the phosphorylation state of tau-protein in the rat brain. Neurobiology of Aging, 19(6), 535-543. https://doi.org/ 10.1016/s0197-4580(98)00094-3 · DOI
  28. Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986). Abnormal phosphorylation of the microtubule- associated protein tau (tau) in Alzheimer cytoskeletal pathology. Pro- ceedings of the National Academy of Sciences of the United States of America, 83(13), 4913-4917.
  29. aad7038 · DOI · Paper page
  30. Hanger, D. P., Goniotaki, D., & Noble, W. (2019). Synaptic localisation of tau. Advances in Experimental Medicine and Biology, 1184, 105-112. https://doi.org/10.1007/978-981-32-9358-8_9 · DOI
  31. Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., Hackett, J., Adamson, J., Lincoln, S., Dickson, D., Davies, P., Petersen, R. C., Stevens, M., de Graaff, E., Wauters, E., … Heutink, P. (1998). Association of missense and 5 0 -splice-site mutations in tau with the inherited dementia FTDP-17. Nature, 393(6686), 702-705. https:// doi.org/10.1038/31508 · DOI · Paper page
  32. Ihara, Y., Nukina, N., Miura, R., & Ogawara, M. (1986). Phosphorylated tau protein is integrated into paired helical filaments in Alzheimer's dis- ease. Journal of Biochemistry, 99(6), 1807-1810.
  33. Irving, E. A., McCulloch, J., & Dewar, D. (1996). Intracortical perfusion of glutamate in vivo induces alterations of tau and microtubule- associated protein 2 immunoreactivity in the rat. Acta Neuropatholo- gica, 92(2), 186-196. https://doi.org/10.1007/s004010050507 · DOI
  34. Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. D. J., Napier, I. A., Eckert, A., Staufenbiel, M., Hardeman, E., & Gotz, J. (2010). Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. Cell, 142(3), 387-397. https://doi.org/10.1016/j.cell.2010. 06.036 · DOI · Paper page
  35. Jadhav, S., Cubinkova, V., Zimova, I., Brezovakova, V., Madari, A., Cigankova, V., & Zilka, N. (2015). Tau-mediated synaptic damage in Alzheimer's disease. Translational Neuroscience, 6(1), 214-226. https:// doi.org/10.1515/tnsci-2015-0023 · DOI
  36. Kanaan, N. M., & Grabinski, T. (2021). Neuronal and glial distribution of tau protein in the adult rat and monkey. Frontiers in Molecular Neuro- science, 14, 607303. https://doi.org/10.3389/fnmol.2021.607303 · DOI · Paper page
  37. Kempf, M., Clement, A., Faissner, A., Lee, G., & Brandt, R. (1996). Tau binds to the distal axon early in development of polarity in a microtubule- and microfilament-dependent manner. The Journal of Neuroscience, 16(18), 5583-5592.
  38. Klein, C., Kramer, E. M., Cardine, A. M., Schraven, B., Brandt, R., & Trotter, J. (2002). Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. The Jour- nal of Neuroscience, 22(3), 698-707.
  39. Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986). Microtubule-associated protein tau (tau) is a major antigenic component of paired helical fila- ments in Alzheimer disease. Proceedings of the National Academy of Sci- ences of the United States of America, 83(11), 4044-4048.
  40. Kubo, A., Misonou, H., Matsuyama, M., Nomori, A., Wada-Kakuda, S., Takashima, A., Kawata, M., Murayama, S., Ihara, Y., & Miyasaka, T. (2019). Distribution of endogenous normal tau in the mouse brain. The Journal of Comparative Neurology, 527(5), 985-998. https://doi.org/ 10.1002/cne.24577 · DOI · Paper page
  41. Kubo, A., Ueda, S., Yamane, A., Wada-Kakuda, S., Narita, M., Matsuyama, M., Nomori, A., Takashima, A., Kato, T., Onodera, O., Goto, M., Ito, M., Tomiyama, T., Mori, H., Murayama, S., Ihara, Y., Misonou, H., & Miyasaka, T. (2019). Ectopic expression induces abnor- mal Somatodendritic distribution of tau in the mouse brain. The Journal of Neuroscience, 39(34), 6781-6797. https://doi.org/10.1523/ jneurosci.2845-18.2019 · DOI
  42. Lee, G., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998). Tau interacts with src-family non-receptor tyrosine kinases. Journal of Cell Science, 111(Pt 21), 3167-3177.
  43. Li, X., Kumar, Y., Zempel, H., Mandelkow, E. M., Biernat, J., & Mandelkow, E. (2011). Novel diffusion barrier for axonal retention of tau in neurons and its failure in neurodegeneration. The EMBO Journal, 30(23), 4825-4837. https://doi.org/10.1038/emboj.2011.376 · DOI
  44. Loomis, P. A., Howard, T. H., Castleberry, R. P., & Binder, L. I. (1990). Iden- tification of nuclear tau isoforms in human neuroblastoma cells. Pro- ceedings of the National Academy of Sciences of the United States of America, 87(21), 8422-8426.
  45. LoPresti, P. (2002). Regulation and differential expression of tau mRNA isoforms as oligodendrocytes mature in vivo: Implications for myelination. Glia, 37(3), 250-257. https://doi.org/10.1002/ glia.10035 · DOI · Paper page
  46. LoPresti, P. (2015). Inducible expression of a truncated form of tau in oli- godendrocytes elicits gait abnormalities and a decrease in myelin: Implications for selective CNS degenerative diseases. Neurochemical Research, 40, 2188-2199. https://doi.org/10.1007/s11064-015- 1707-x · DOI
  47. LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I. (1995). Functional implications for the microtubule- associated protein tau: Localization in oligodendrocytes. Proceedings of the National Academy of Sciences of the United States of America, 92(22), 10369-10373.
  48. Mandell, J. W., & Banker, G. A. (1996). A spatial gradient of tau protein phosphorylation in nascent axons. The Journal of Neuroscience, 16(18), 5727-5740.
  49. Migheli, A., Butler, M., Brown, K., & Shelanski, M. L. (1988). Light and elec- tron microscope localization of the microtubule-associated tau protein in rat brain. The Journal of Neuroscience, 8(6), 1846-1851.
  50. Mondragon-Rodriguez, S., Trillaud-Doppia, E., Dudilot, A., Bourgeois, C., Lauzon, M., Leclerc, N., & Boehm, J. (2012). Interaction of endogenous tau protein with synaptic proteins is regulated by N-methyl- D-aspartate receptor-dependent tau phosphorylation. The Journal of Biological Chemistry, 287(38), 32040-32053. https://doi.org/10.1074/ jbc.M112.401240 · DOI · Paper page
  51. Mueller, R. L., Combs, B., Alhadidy, M. M., Brady, S. T., Morfini, G. A., & Kanaan, N. M. (2021). Tau: A signaling hub protein. Frontiers in Molecu- lar Neuroscience, 14, 647054. https://doi.org/10.3389/fnmol.2021. 647054 · DOI
  52. Nukina, N., & Ihara, Y. (1986). One of the antigenic determinants of paired helical filaments is related to tau protein. Journal of Biochemistry, 99(5), 1541-1544.
  53. Papasozomenos, S. C., & Binder, L. I. (1987). Phosphorylation determines two distinct species of tau in the central nervous system. Cell Motility and the Cytoskeleton, 8(3), 210-226. https://doi.org/10.1002/cm. 970080303 · DOI · Paper page
  54. Paterno, G., Bell, B. M., Gorion, K. M., Prokop, S., & Giasson, B. I. (2022). Reassessment of neuronal tau distribution in adult human brain and implications for tau pathobiology. Acta Neuropathologica Communica- tions, 10(1), 94. https://doi.org/10.1186/s40478-022-01394-9 · DOI
  55. Robbins, M., Clayton, E., & Kaminski Schierle, G. S. (2021). Synaptic tau: A pathological or physiological phenomenon? Acta Neuropathologica Communications, 9(1), 149. https://doi.org/10.1186/s40478-021- 01246-y · DOI
  56. Schaler, A. W., Runyan, A. M., Clelland, C. L., Sydney, E. J., Fowler, S. L., Figueroa, H. Y., Shioda, S., Santa-Maria, I., Duff, K. E., & Myeku, N. (2021). PAC1 receptor-mediated clearance of tau in postsynaptic com- partments attenuates tau pathology in mouse brain. Science Transla- tional Medicine, 13(595), 1-15. https://doi.org/10.1126/scitranslmed. · DOI
  57. aba7394 · DOI
  58. Seiberlich, V., Bauer, N. G., Schwarz, L., Ffrench-Constant, C., Goldbaum, O., & Richter-Landsberg, C. (2015). Downregulation of the microtubule associated protein tau impairs process outgrowth and myelin basic protein mRNA transport in oligodendrocytes. Glia, 63(9), 1621-1635. https://doi.org/10.1002/glia.22832 · DOI · Paper page
  59. Sohn, P. D., Tracy, T. E., Son, H. I., Zhou, Y., Leite, R. E., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016). Acetylated tau desta- bilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment. Molecular Neurodegeneration, 11(1), 47. https://doi.org/10.1186/s13024-016-0109-0 · DOI · Paper page
  60. Sündermann, F., Fernandez, M. P., & Morgan, R. O. (2016). An evolutionary roadmap to the microtubule-associated protein MAP tau. BMC Geno- mics, 17, 264. https://doi.org/10.1186/s12864-016-2590-9 · DOI
  61. Tai, H. C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires- Jones, T. L., & Hyman, B. T. (2012). The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. The American Journal of Pathology, 181(4), 1426-1435. https://doi.org/10.1016/j. ajpath.2012.06.033 · DOI
  62. Takahashi, M., Tomizawa, K., & Ishiguro, K. (2000). Distribution of tau pro- tein kinase I/glycogen synthase kinase-3beta, phosphatases 2A and 2B, and phosphorylated tau in the developing rat brain. Brain Research, 857(1-2), 193-206. https://doi.org/10.1016/s0006-8993(99) 02424-5 · DOI
  63. Tashiro, K., Hasegawa, M., Ihara, Y., & Iwatsubo, T. (1997). Somatodendri- tic localization of phosphorylated tau in neonatal and adult rat cerebral cortex. Neuroreport, 8(12), 2797-2801. https://doi.org/10.1097/ 00001756-199708180-00029 · DOI
  64. Thurston, V. C., Pena, P., Pestell, R., & Binder, L. I. (1997). Nucleolar locali- zation of the microtubule-associated protein tau in neuroblastomas using sense and anti-sense transfection strategies. Cell Motility and the Cytoskeleton, 38(1), 100-110. https://doi.org/10.1002/(sici)1097- 0169(1997)38:1<100::aid-cm9>3.0.co;2-c · DOI
  65. Thurston, V. C., Zinkowski, R. P., & Binder, L. I. (1996). Tau as a nucleolar protein in human nonneural cells in vitro and in vivo. Chromosoma, 105(1), 20-30.
  66. Tjiang, N., & Zempel, H. (2022). A mitochondria cluster at the proximal axon initial segment controls axodendritic TAU trafficking in rodent primary and human iPSC-derived neurons. Cellular and Molecular Life Sciences, 79(2), 120. https://doi.org/10.1007/s00018-022-04150-3 · DOI
  67. Trushina, N. I., Bakota, L., Mulkidjanian, A. Y., & Brandt, R. (2019). The evo- lution of tau phosphorylation and interactions. Frontiers in Aging Neu- roscience, 11, 256. https://doi.org/10.3389/fnagi.2019.00256 · DOI
  68. Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., Buée, L., & Galas, M. C. (2014). A major role for tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic con- ditions. Frontiers in Cellular Neuroscience, 8, 84. https://doi.org/10. 3389/fncel.2014.00084 · DOI · Paper page
  69. Wang, Y., & Mandelkow, E. (2016). Tau in physiology and pathology. Nature Reviews. Neuroscience, 17(1), 22-35. https://doi.org/10.1038/ nrn.2015.1031 · DOI
  70. Wei, Y., Qu, M. H., Wang, X. S., Chen, L., Wang, D. L., Liu, Y., Hua, Q., & He, R. Q. (2008). Binding to the minor groove of the double-strand, tau protein prevents DNA from damage by peroxidation. PLoS One, 3(7), e2600. https://doi.org/10.1371/journal.pone.0002600 · DOI · Paper page
  71. Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975). A protein factor essential for microtubule assembly. Proceed- ings of the National Academy of Sciences of the United States of America, 72(5), 1858-1862.
  72. Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986). Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axo- nal microtubule-associated protein tau (tau). Proceedings of the National Academy of Sciences of the United States of America, 83(11), 4040-4043.
  73. Ximerakis, M., Lipnick, S. L., Innes, B. T., Simmons, S. K., Adiconis, X., Dionne, D., Mayweather, B. A., Nguyen, L., Niziolek, Z., Ozek, C., Butty, V. L., Isserlin, R., Buchanan, S. M., Levine, S. S., Regev, A., Bader, G. D., Levin, J. Z., & Rubin, L. L. (2019). Single-cell transcrip- tomic profiling of the aging mouse brain. Nature Neuroscience, 22(10), 1696-1708. https://doi.org/10.1038/s41593-019-0491-3 · DOI · Paper page
  74. Zempel, H., Dennissen, F. J. A., Kumar, Y., Luedtke, J., Biernat, J., Mandelkow, E. M., & Mandelkow, E. (2017). Axodendritic sorting and pathological missorting of tau are isoform-specific and determined by axon initial segment architecture. The Journal of Biological Chemistry, 292(29), 12192-12207. https://doi.org/10.1074/jbc.M117.784702 · DOI
  75. Zempel, H., & Mandelkow, E. (2019). Mechanisms of axonal sorting of tau and influence of the axon initial segment on tau cell polarity. Advances in Experimental Medicine and Biology, 1184, 69-77. https://doi.org/10. 1007/978-981-32-9358-8_6 · DOI

Cited by

Sorted by citations

Authors
Kanaan, N. M.
Affiliations
Michigan State University (US)
Corresponding author
Kanaan, Nicholas M.
ORCID
Kanaan, Nicholas M.
Venue
Cytoskeleton
Publisher
Wiley
Published
2023-12-16
Volume
81
Issue
1
Pages
107-115
ISSN
  • 1949-3584 (ISSN-L)
  • 1949-3592
DOI
10.1002/cm.21820
PMC
PMC10851165
OpenAlex
W4389828626
Cited by
15
References
10
Citations by year
2026: 9 · 2025: 6
FWCI
2.66
Type
journal article
Language
en
Open access
Licence
Locations
  • Cytoskeleton (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion, cc-by)
Funders
  • National Institute of Neurological Disorders and Stroke (R01 NS082730)
  • National Institute on Aging (R01 AG044372, R01 AG067762, P30 AG072931)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords
tau protein, subcellular localization, adult central nervous system, neuronal somata, dendrites, synapses, glial cells, Alzheimer's disease
MeSH terms
Axons, Microtubules, Neurons, Synapses, tau Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review