Wikipedia

MAPT

MAPT (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[55][56]

MAPT
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген Тау-белок[d][1]
Молекуляр функция apolipoprotein binding[d][2], SH3 domain binding[d][3], tubulin binding[d][4], связывание с белками плазмы[d][5][6][7][…], lipoprotein particle binding[d][8], enzyme binding[d][9][10][11], ДНК-связывающий[d][12], actin binding[d][13][14][15], microtubule binding[d][16][12][17], dynactin binding[d][18], receptor ligand activity[d][16][19], protein phosphatase 2A binding[d][18], Hsp90 protein binding[d][12], ДНК-связывающий[d][15][4], minor groove of adenine-thymine-rich DNA binding[d][15], double-stranded DNA binding[d][15], single-stranded DNA binding[d][15], RNA binding[d][15], microtubule binding[d][18][20][15][…], enzyme binding[d][21][22][23][…], protein kinase binding[d][24][25], protein-macromolecule adaptor activity[d][15], phosphatidylinositol binding[d][15], связывание похожих белков[d][7][26][27], гомодимеризация белка[d][28], sequence-specific DNA binding[d][15], receptor ligand activity[d][29], chaperone binding[d][30], Hsp90 protein binding[d][31], histone-dependent DNA binding[d][15], microtubule lateral binding[d][32] һәм phosphatidylinositol bisphosphate binding[d][15]
Күзәнәк компоненты цитоплазма[12], cell body[d][33], cell projection[d][4], nuclear periphery[d][34], Конус роста[d][35], Нейрофибриллярный клубок[d][33], күзәнәк мембранасы[d][12][36][12], tubulin complex[d][35], дендрит[d][33], cytoplasmic ribonucleoprotein granule[d][37], цитоскелет[d][4], төш[12], цитозоль[d][12][12][12], микротрубочка[d][16][12], microtubule associated complex[d][12], мембрана[d][38][4], ядерные спеклы[d][4], аксон[d][16][12][39], somatodendritic compartment[d][40], soma[d][38], axon cytoplasm[d][4], күзәнәк тышындагы өлкә[d][15], внутренний компонент клетки[d][41][15], төш[15][4], цитоплазма[4][7][4][…], митохондрия[15], цитозоль[d][4][4][4][…], микротрубочка[d][4][4], күзәнәк мембранасы[d][15][4][42][…], microtubule cytoskeleton[d][18][15][43][…], аксон[d][15][18][4][…], дендрит[d][4][44][45], axolemma[d][46], somatodendritic compartment[d][15][38], neuron projection[d][47], дендритный шипик[d][15], cell body[d][4][45], main axon[d][4], липидный рафт[d][4], glial cell projection[d][4] һәм Нейрофибриллярный клубок[d][45][48]
Биологик процесс Lua хатасы: too many expensive function calls.
Изображение Gene Atlas

Искәрмәләр

үзгәртү
  1. ↑ 1,0 1,1 UniProt
  2. ↑ Roses A. D., Saunders A. M. ApoE3 binding to tau tandem repeat I is abolished by tau serine262 phosphorylation // Neurosci. Lett. — Elsevier BV, 1995. — ISSN 0304-3940; 1872-7972 — doi:10.1016/0304-3940(95)11649-H — PMID:7566652
  3. ↑ Lee G, ST N., DL G. et al. Tau interacts with src-family non-receptor tyrosine kinases // J. Cell Sci. — The Company of Biologists, 1998. — ISSN 0021-9533; 1477-9137 — PMID:9763511
  4. ↑ 4,00 4,01 4,02 4,03 4,04 4,05 4,06 4,07 4,08 4,09 4,10 4,11 4,12 4,13 4,14 4,15 4,16 4,17 4,18 4,19 4,20 4,21 GOA
  5. ↑ A. Takashima, M. Murayama, O. Murayama et al. Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau, Presenilin 1 associates with glycogen synthase kinase-3β and its substrate tau // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1998. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.95.16.9637 — PMID:9689133
  6. ↑ Geetha T. Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation // J. Neurochem. — Wiley-Blackwell, 2005. — ISSN 0022-3042; 1471-4159 — doi:10.1111/J.1471-4159.2005.03181.X — PMID:15953362
  7. ↑ 7,0 7,1 7,2 Guerreiro P. S. LRRK2 Promotes Tau Accumulation, Aggregation and Release // Mol. Neurobiol. — Springer Science+Business Media, 2015. — ISSN 0893-7648; 1559-1182 — doi:10.1007/S12035-015-9209-Z — PMID:26014385
  8. ↑ M Pericak-Vance, Roses A. D., Saunders A. M. Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1994. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.91.23.11183 — PMID:7972031
  9. ↑ Baulieu E., Dounane O. A role for FKBP52 in Tau protein function // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2010. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0914957107 — PMID:20133804
  10. ↑ Binder L. I. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1630428100 — PMID:12888622
  11. ↑ Brancolini C. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis // J. Neurosci. / M. Picciotto — Society for Neuroscience, 1998. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.18-18-07061.1998 — PMID:9736630
  12. ↑ 12,00 12,01 12,02 12,03 12,04 12,05 12,06 12,07 12,08 12,09 12,10 12,11 12,12 12,13 GOA
  13. ↑ Bodea L., Eckert A., Götz J. et al. Tau physiology and pathomechanisms in frontotemporal lobar degeneration // J. Neurochem. — Wiley-Blackwell, 2016. — 24 p. — ISSN 0022-3042; 1471-4159 — doi:10.1111/JNC.13600 — PMID:27306859
  14. ↑ 14,0 14,1 14,2 Götz J. Tau promotes neurodegeneration via DRP1 mislocalization in vivo // Neuron / K. Brose — Cell Press, Elsevier BV, 2012. — ISSN 0896-6273; 1097-4199 — doi:10.1016/J.NEURON.2012.06.026 — PMID:22920254
  15. ↑ 15,00 15,01 15,02 15,03 15,04 15,05 15,06 15,07 15,08 15,09 15,10 15,11 15,12 15,13 15,14 15,15 15,16 15,17 15,18 15,19 15,20 Guo T., Noble W., Hanger D. P. Roles of tau protein in health and disease // Acta Neuropathol. (Berl) — Springer Science+Business Media, 2017. — ISSN 0001-6322; 1432-0533 — doi:10.1007/S00401-017-1707-9 — PMID:28386764
  16. ↑ 16,0 16,1 16,2 16,3 16,4 Yu J., Tan L. The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy // Mol. Neurobiol. — Springer Science+Business Media, 2016. — ISSN 0893-7648; 1559-1182 — doi:10.1007/S12035-015-9415-8 — PMID:26363795
  17. ↑ Butner K. A., Kirschner M. W. Tau protein binds to microtubules through a flexible array of distributed weak sites // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 1991. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.115.3.717 — PMID:1918161
  18. ↑ 18,00 18,01 18,02 18,03 18,04 18,05 18,06 18,07 18,08 18,09 18,10 Yu J., Tan L. The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy // Mol. Neurobiol. — Springer Science+Business Media, 2016. — ISSN 0893-7648; 1559-1182 — doi:10.1007/S12035-015-9415-8 — PMID:26363795
  19. ↑ Diaz-Hernandez M., María Teresa Miras Portugal Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells // Mol. Cell. Neurosci. — Elsevier BV, 2007. — ISSN 1044-7431; 1095-9327 — doi:10.1016/J.MCN.2007.12.010 — PMID:18272392
  20. ↑ Atapour N., Hensch T. K., Hirokawa N. Defects in Synaptic Plasticity, Reduced NMDA-Receptor Transport, and Instability of Postsynaptic Density Proteins in Mice Lacking Microtubule-Associated Protein 1A // J. Neurosci. / M. Picciotto — Society for Neuroscience, 2015. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.2671-15.2015 — PMID:26609151
  21. ↑ Plattner F. Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2013. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M112.433326 — PMID:23362255
  22. ↑ Binder L. I. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2003. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1630428100 — PMID:12888622
  23. ↑ Brancolini C. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis // J. Neurosci. / M. Picciotto — Society for Neuroscience, 1998. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.18-18-07061.1998 — PMID:9736630
  24. ↑ Ryoo S., Jeong H. K., Radnaabazar C. et al. DYRK1A-mediated hyperphosphorylation of Tau. A functional link between Down syndrome and Alzheimer disease // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2007. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M707358200 — PMID:17906291
  25. ↑ Zweckstetter M., Mandelkow E., Blackledge M. Phosphorylation of human Tau protein by microtubule affinity-regulating kinase 2. // Biochemistry / A. Schepartz — ACS, 2013. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI401266N — PMID:24251416
  26. ↑ O. Schweers, E. Schönbrunn-Hanebeck, A. Marx et al. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1994. — ISSN 0021-9258; 1083-351X; 1067-8816 — PMID:7929085
  27. ↑ Mandelkow E. Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain // Biochemistry / A. Schepartz — ACS, 2004. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI0357006 — PMID:14769047
  28. ↑ Eliezer D., Barré P., Kobaslija M. et al. Residual structure in the repeat domain of tau: echoes of microtubule binding and paired helical filament formation // Biochemistry / A. Schepartz — ACS, 2005. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI048953N — PMID:15654759
  29. ↑ Diaz-Hernandez M., María Teresa Miras Portugal Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells // Mol. Cell. Neurosci. — Elsevier BV, 2007. — ISSN 1044-7431; 1095-9327 — doi:10.1016/J.MCN.2007.12.010 — PMID:18272392
  30. ↑ Zhou Y., Hayashi I., Wong J. et al. Intracellular clusterin interacts with brain isoforms of the bridging integrator 1 and with the microtubule-associated protein Tau in Alzheimer's disease // PLOS ONE / PLOS ONE Editors — PLoS, 2014. — ISSN 1932-6203 — doi:10.1371/JOURNAL.PONE.0103187 — PMID:25051234
  31. ↑ Chiosis G., Greengard P. Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2007. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0701055104 — PMID:17517623
  32. ↑ Mandelkow E., Hoenger A., Skiniotis G. Surface-decoration of microtubules by human tau // Journal of Molecular Biology / P. Wright — Elsevier BV, 2004. — ISSN 0022-2836; 1089-8638 — doi:10.1016/J.JMB.2004.04.008 — PMID:15147841
  33. ↑ 33,0 33,1 33,2 Cummings D. M., Muzammil A Nahaboo Solim, Moens T. G. et al. A genome-wide gene-expression analysis and database in transgenic mice during development of amyloid or tau pathology // Cell Reports — Cell Press, Elsevier BV, 2015. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2014.12.041 — PMID:25620700
  34. ↑ Dinh K., Poindexter B. J., Barnes J. L. et al. Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells // Cytokine — Elsevier BV, 2009. — ISSN 1043-4666; 1096-0023 — doi:10.1016/J.CYTO.2008.12.004 — PMID:19157893
  35. ↑ 35,0 35,1 Black M. M., T Slaughter, S Moshiach et al. Tau is enriched on dynamic microtubules in the distal region of growing axons // J. Neurosci. / M. Picciotto — Society for Neuroscience, 1996. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.16-11-03601.1996 — PMID:8642405
  36. ↑ Lee G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 1995. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.131.5.1327 — PMID:8522593
  37. ↑ Villacé P., Marión R. M., Ortín J. The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs // Nucleic Acids Res. — OUP, University of Oxford, 2004. — ISSN 0305-1048; 1362-4962; 1362-4954 — doi:10.1093/NAR/GKH552 — PMID:15121898
  38. ↑ 38,0 38,1 38,2 38,3 38,4 Ittner L. M., Ke Y. D., Delerue F. et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models // Cell — Cell Press, Elsevier BV, 2010. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2010.06.036 — PMID:20655099
  39. ↑ Black M. M., T Slaughter, S Moshiach et al. Tau is enriched on dynamic microtubules in the distal region of growing axons // J. Neurosci. / M. Picciotto — Society for Neuroscience, 1996. — ISSN 0270-6474; 1529-2401 — doi:10.1523/JNEUROSCI.16-11-03601.1996 — PMID:8642405
  40. ↑ Ittner L. M., Ke Y. D., Delerue F. et al. Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models // Cell — Cell Press, Elsevier BV, 2010. — ISSN 0092-8674; 1097-4172 — doi:10.1016/J.CELL.2010.06.036 — PMID:20655099
  41. ↑ Deaconescu A. M., Kutter S. Regulation of Microtubule Assembly by Tau and not by Pin1. // Journal of Molecular Biology / P. Wright — Elsevier BV, 2016. — ISSN 0022-2836; 1089-8638 — doi:10.1016/J.JMB.2016.03.010 — PMID:26996940
  42. ↑ 42,0 42,1 Lee G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 1995. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.131.5.1327 — PMID:8522593
  43. ↑ Miller B. L., Seeley W. W. Acetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment // Mol. Neurodegener. — BMC, Springer Science+Business Media, 2016. — ISSN 1750-1326 — doi:10.1186/S13024-016-0109-0 — PMID:27356871
  44. ↑ Landegren U., Lund H., Gu G. J. et al. Role of individual MARK isoforms in phosphorylation of tau at Ser²⁶² in Alzheimer's disease // Neuromol. Med. — Springer Science+Business Media, 2013. — ISSN 1535-1084; 1559-1174 — doi:10.1007/S12017-013-8232-3 — PMID:23666762
  45. ↑ 45,0 45,1 45,2 Cummings D. M., Muzammil A Nahaboo Solim, Moens T. G. et al. A genome-wide gene-expression analysis and database in transgenic mice during development of amyloid or tau pathology // Cell Reports — Cell Press, Elsevier BV, 2015. — ISSN 2211-1247; 2639-1856 — doi:10.1016/J.CELREP.2014.12.041 — PMID:25620700
  46. ↑ T Maas, J Eidenmüller, R Brandt Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2000. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M000389200 — PMID:10747907
  47. ↑ Livstone M. S., Thomas P. D., Lewis S. E. et al. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium // Brief. Bioinform. — OUP, 2011. — ISSN 1467-5463; 1477-4054 — doi:10.1093/BIB/BBR042 — PMID:21873635
  48. ↑ M. Goedert, Spillantini M. G., R. Jakes et al. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease // Neuron / K. Brose — Cell Press, Elsevier BV, 1989. — ISSN 0896-6273; 1097-4199 — doi:10.1016/0896-6273(89)90210-9 — PMID:2484340
  49. ↑ Elrick M. J. Tau deletion exacerbates the phenotype of Niemann-Pick type C mice and implicates autophagy in pathogenesis // Human Molecular Genetics — OUP, 2008. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDN423 — PMID:19074461
  50. ↑ 50,0 50,1 Weingarten M. D., Lockwood A. H., Hwo S. Y. et al. A protein factor essential for microtubule assembly // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1975. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.72.5.1858 — PMID:1057175
  51. ↑ Drechsel D. N., Hyman A. A., Cobb M. H. et al. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau // Mol. Biol. Cell, — American Society for Cell Biology, 1992. — ISSN 1059-1524; 1939-4586; 1044-2030 — doi:10.1091/MBC.3.10.1141 — PMID:1421571
  52. ↑ Mandelkow E., Mandelkow E., G Drewes et al. Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 1995. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.270.13.7679 — PMID:7706316
  53. ↑ A. Caceres, J. Mautino, Kosik K. S. Suppression of MAP2 in cultured cerebellar macroneurons inhibits minor neurite formation // Neuron / K. Brose — Cell Press, Elsevier BV, 1992. — ISSN 0896-6273; 1097-4199 — doi:10.1016/0896-6273(92)90025-9 — PMID:1389180
  54. ↑ Ludvigson A. E., Luebke J., Spires-Jones T. L. et al. Tau accumulation causes mitochondrial distribution deficits in neurons in a mouse model of tauopathy and in human Alzheimer's disease brain // Am. J. Pathol. — Elsevier BV, 2011. — ISSN 0002-9440; 1525-2191; 0097-3599 — doi:10.1016/J.AJPATH.2011.07.004 — PMID:21854751
  55. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  56. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар

үзгәртү
  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)


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Чыганак — https://tt.wikipedia.org/w/index.php?title=MAPT&oldid=4131020