The MAP1 family of microtubule-associated proteins.
Open accessAbstract
Microtubule-associated proteins (MAPs) of the MAP2/Tau family include the vertebrate proteins MAP2, MAP4, and Tau and homologs in other animals. All three vertebrate members of the family have alternative splice forms; all isoforms share a conserved carboxy-terminal domain containing microtubule-binding repeats, and an amino-terminal projection domain of varying size. MAP2 and Tau are found in neurons, whereas MAP4 is present in many other tissues but is generally absent from neurons. Members of the family are best known for their microtubule-stabilizing activity and for proposed roles regulating microtubule networks in the axons and dendrites of neurons. Contrary to this simple, traditional view, accumulating evidence suggests a much broader range of functions, such as binding to filamentous (F) actin, recruitment of signaling proteins, and regulation of microtubule-mediated transport. Tau is also implicated in Alzheimer's disease and other dementias. The ability of MAP2 to interact with both microtubules and F-actin might be critical for neuromorphogenic processes, such as neurite initiation, during which networks of microtubules and F-actin are reorganized in a coordinated manner. Various upstream kinases and interacting proteins have been identified that regulate the microtubule-stabilizing activity of MAP2/Tau family proteins.
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Tau belongs to a family of microtubule-associated proteins including MAP2, which is prevalently expressed in neurons.
“Tau belongs to a family of microtubule-associated proteins including MAP2, a protein that is also prevalently expressed in neurons (28).”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [28]
The primary function of MAP2, like Tau, is thought to be binding to MT to stabilize them.
“The Primary function of MAP2, like Tau, is thought to be binding to MT to stabilize them (3).”
From Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons (2026) · cites this paper as [3]
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Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works
MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., & Milligan, R. A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201048 · Cited by 327 · see citing works
Self-citationSingle-molecule investigation of the interference between kinesin, tau and MAP2c
Seitz, A., Kojima, H., Oiwa, K., Mandelkow, E.-M., Song, Y.-H., & Mandelkow, E. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf503 · Cited by 257 · see citing works
Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179 · see citing works
Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144 · cited 1× · see citing works
“[26], differential protein sorting [27], and dendrite-specific transport of MAP2 mRNA [28] are responsible for this spatial segregation of the two MAPs.”
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Research works printed but not linked: 79
- Hale CA de Boer PA Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 1997 88 175 185 The interaction between the bacterial tubulin homolog FtsZ and an ancestral MAP, ZipA, is described. 9008158 10.1016/S0092-8674(00)81838-3 · DOI
- RayChaudhuri D ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J 1999 18 2372 2383 The functional significance of the ancestral MAP ZipA in bacterial cell division is described and its relation to MAP2/Tau is proposed. 10228152 10.1093/emboj/18.9.2372 PMC1171320 · DOI
- Hale CA Rhee AC de Boer PA ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J Bacteriol 2000 182 5153 5166 The FtsZ interaction domain on ZipA is mapped to its carboxyl terminus, a region unrelated to MAP2/Tau, suggesting that ZipA is not a functional homolog of MAP2/Tau proteins. 10960100 10.1128/JB.182.18.5153-5166.2000 PMC94664 · DOI
- Goedert M Baur CP Ahringer J Jakes R Hasegawa M Spillantini MG Smith MJ Hill F PTL-1, a microtubule-associated protein with tau-like repeats from the nematode Caenorhabditis elegans. J Cell Sci 1996 109 2661 2672 Describes the cloning of a MAP2/Tau homolog from C. elegans, expression analyses, microtubule binding and stabilization experiments, and overexpression studies. 8937984
- McDermott JB Aamodt S Aamodt E ptl-1, a Caenorhabditis elegans gene whose products are homologous to the tau microtubule-associated proteins. Biochemistry 1996 35 9415 9423 The first characterization and cloning of the C. elegans MAP2/Tau homolog. 8755720 10.1021/bi952646n · DOI
- Heidary G Fortini ME Identification and characterization of the Drosophila tau homolog. Mech Dev 2001 108 171 178 Cloning, expression and subcellular localization studies of the fly MAP2/Tau homolog are described. 11578871 10.1016/S0925-4773(01)00487-7 · DOI
- Kalcheva N Albala J O'Guin K Rubino H Garner C Shafit-Zagardo B Genomic structure of human microtubule-associated protein 2 (MAP-2) and characterization of additional MAP-2 isoforms. Proc Natl Acad Sci USA 1995 92 10894 10898 The human MAP2 gene is sequenced and analyzed and additional splice forms are characterized. 7479905 PMC40537
- Himmler A Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family. Mol Cell Biol 1989 9 1389 1396 The bovine Tau gene is sequenced and analyzed and additional splice forms are described. 2498650 PMC362555
- Lewis SA Wang D Cowan NJ Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein. Science 1988 242 936 939 This paper defined the relationship between MAP2 and Tau and thereby defined the MAP2/Tau family by showing that the two proteins contain related microtubule-binding domains. 3142041
- Ozer RS Halpain S Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton. Mol Biol Cell 2000 11 3573 3587 The phosphorylation of MAP2c by PKA and its relevance for MAP2-microtubule and MAP2-F-actin interaction is reported. 11029056 PMC15014
- Drewes G Trinczek B Illenberger S Biernat J Schmitt-Ulms G Meyer HE Mandelkow EM Mandelkow E 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 1995 270 7679 7688 Purification of a novel kinase and characterization of its role in regulating the microtubule-Tau interaction. 7706316 10.1074/jbc.270.13.7679 · DOI · Paper page
- Mukhopadhyay R Hoh JH AFM force measurements on microtubule-associated proteins: the projection domain exerts a long-range repulsive force. FEBS Lett 2001 505 374 378 The authors measured a repulsive, entropic force generated by arrays of bovine brain MAPs (of which 70% was made up of the MAP2a and MAP2b isoforms). 11576531 10.1016/S0014-5793(01)02844-7 · DOI · Paper page
- Uversky VN What does it mean to be natively unfolded? Eur J Biochem 2002 269 2 12 A review of the basic biochemical characteristics of natively unfolded proteins, such as the MAP2/Tau proteins. 11784292 10.1046/j.0014-2956.2001.02649.x · DOI
- Malmendal A Halpain S Chazin WJ Nascent structure in the kinase anchoring domain of microtubule-associated protein 2. Biochem Biophys Res Commun 2003 301 136 142 Characterization of the structural properties of the PKA-RII-binding domain of MAP2 using limited proteolysis, nuclear magnetic resonance spectroscopy and circular dichroism spectroscopy. 12535652 10.1016/S0006-291X(02)02989-3 · DOI
- Roger B Al Bassam J Dehmelt L Milligan RA Halpain S MAP2c, but not tau, binds and bundles F-actin via its microtubule binding domain. Curr Biol 2004 14 363 371 This key paper demonstrates that binding of MAP2/Tau proteins to F-actin correlates with their ability to induce neurites. It is also the first paper to measure this binding quantitatively. 15028210 10.1016/j.cub.2004.01.058 · DOI · Paper page
- Menezes JR Luskin MB Expression of neuron-specific tubulin defines a novel population in the proliferative layers of the developing telencephalon. J Neurosci 1994 14 5399 5416 The temporal sequence of expression of neuronal markers β-III-tubulin and MAP2 is analyzed with respect to the behavior of migrating neurons and dividing neuronal precursors in the developing brain. 8083744 PMC6577108
- Garner CC Brugg B Matus A A 70-kilodalton microtubule-associated protein (MAP2c), related to MAP2. J Neurochem 1988 50 609 615 The cloning and characterization of the small MAP2 isoform MAP2c is reported. 3121794
- Chung WJ Kindler S Seidenbecher C Garner CC MAP2a, An alternatively spliced variant of microtubule associated protein 2. J Neurochem 1996 66 1273 1281 The cloning and characterization of the alternatively spliced adult MAP2 isoform MAP2a is described. 8769894
- Goedert M Spillantini MG Jakes R Rutherford D Crowther RA Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 1989 3 519 26 Characterization using RNAse protection assays of developmentally regulated isoforms of Tau that differ in the number of microtubule-binding repeats. 2484340 10.1016/0896-6273(89)90210-9 · DOI · Paper page
- Kosik KS Orecchio LD Bakalis S Neve RL Developmentally regulated expression of specific tau sequences. Neuron 1989 2 1389 1397 Identification of isoforms of Tau and their developmental expression, using northern blots. 2560640 10.1016/0896-6273(89)90077-9 · DOI
- Mavilia C Couchie D Nunez J Diversity of high-molecular-weight tau proteins in different regions of the nervous system. J Neurochem 1994 63 2300 2306 An analysis of the regional expression of specific high-molecular-weight Tau splice forms. 7964751
- Kotani S Murofushi H Maekawa S Aizawa H Sakai H Isolation of rat liver microtubule-associated proteins. Evidence for a family of microtubule-associated proteins with molecular mass of around 200,000 which distribute widely among mammalian cells. J Biol Chem 1988 263 5385 5389 Cloning of MAP4 and analysis of its tissue expression. 3356691
- Parysek LM del Cerro M Olmsted JB Microtubule-associated protein 4 antibody: a new marker for astroglia and oligodendroglia. Neuroscience 1985 15 869 875 The expression of MAP4 in the murine brain is analyzed. 3906429 10.1016/0306-4522(85)90084-3 · DOI
- Matus A Microtubule-associated proteins and the determination of neuronal form. J Physiol (Paris) 1990 84 134 137 A review of the subcellular localization and expression patterns of MAP2/Tau family proteins. 2193146
- Garner CC Tucker RP Matus A Selective localization of messenger RNA for cytoskeletal protein MAP2 in dendrites. Nature 1988 336 674 677 The localization of MAP2 mRNA to dendrites is reported. 3200318 10.1038/336674a0 · DOI
- Hirokawa N Shiomura Y Okabe S Tau proteins: the molecular structure and mode of binding on microtubules. J Cell Biol 1988 107 1449 1459 An ultrastructural analysis of Tau binding to microtubules is reported. 3139677 10.1083/jcb.107.4.1449 PMC2115262 · DOI
- Hirokawa N Hisanaga S-I Shiomura Y MAP2 is a component of crossbridges between microtubules and neurofilaments in the neuronal cytoskeleton: quick-freeze, deep-etch immunoelectron microscopy and reconstitution studies. J Neurosci 1988 8 2769 2779 The structure of MAP2 in microtubule arrays is characterized using electron microscopy. 3045269 PMC6569399
- Felgner H Frank R Biernat J Mandelkow EM Mandelkow E Ludin B Matus A Schliwa M Domains of neuronal microtubule-associated proteins and flexural rigidity of microtubules. J Cell Biol 1997 138 1067 1075 An analysis of the molecular basis of MAP2/Tau-induced flexural rigidity of microtubules using optical tweezers. 9281584 10.1083/jcb.138.5.1067 PMC2136754 · DOI
- Weisshaar B Doll T Matus A Reorganisation of the microtubular cytoskeleton by embryonic microtubule-associated protein 2 (MAP2c). Development 1992 116 1151 1161 The organization of microtubules in non-neuronal cells exogenously expressing MAP2c. 1338311
- Lewis SA Ivanov IE Lee GH Cowan NJ Organization of microtubules in dendrites and axons is determined by a short hydrophobic zipper in microtubule-associated proteins MAP2 and tau. Nature 1989 342 498 505 This paper describes microtubule bundle formation in transfected cells induced by MAP2 and Tau, and a potential mechanism is proposed. See also [35]. 2511449 10.1038/342498a0 · DOI
- Lewis SA Cowan N Microtubule bundling. Nature 1990 345 674 A letter providing additional data leading to a reinterpretation of the proposal in [34]. 2113613 10.1038/345293a0 · DOI
- Burgin KE Ludin B Ferralli J Matus A Bundling of microtubules in transfected cells does not involve an autonomous dimerization site on the MAP2 molecule. Mol Biol Cell 1994 5 511 517 Given the lack of a high-affinity dimerization site on MAP2c, this article proposes that microtubule stabilization by itself, through the physical restraint of the cell borders, is responsible for microtubule bundling. 7919534 PMC301063
- Takemura R Okabe S Umeyama T Hirokawa N Polarity orientation and assembly process of microtubule bundles in nocodazole-treated, MAP2c-transfected COS cells. Mol Biol Cell 1995 6 981 996 MAP2c-induced microtubule bundle assembly is analyzed by live-cell microscopy and the polarity of the resulting bundles is determined by electron microscopy. 7579713 PMC301257
- Dehmelt L Smart FM Ozer RS Halpain S The role of microtubule-associated protein 2c in the reorganization of microtubules and lamellipodia during neurite initiation. J Neurosci 2003 23 9479 9490 Cytoskeletal rearrangements during spontaneous and MAP2c-induced neurite initiation are characterized using live-cell microscopy and MAP2 deletion analysis. 14573527 PMC6740480
- Harada A Oguchi K Okabe S Kuno J Terada S Ohshima T Sato-Yoshitake R Takei Y Noda T Hirokawa N Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 1994 369 488 491 Generation and characterization of a Tau knockout mouse, which has defects in axon ultrastructure. 8202139 10.1038/369488a0 · DOI
- Harada A Teng J Takei Y Oguchi K Hirokawa N MAP2 is required for dendrite elongation, PKA anchoring in dendrites, and proper PKA signal transduction. J Cell Biol 2002 158 541 549 MAP2 knockout mice show defects in dendrite outgrowth and targeting of the RII subunit of PKA to dendrites. 12163474 10.1083/jcb.200110134 PMC2173814 · DOI
- DiTella MC Feiguin F Carri N Kosik KS Caceres A MAP-1B/TAU functional redundancy during laminin-enhanced axonal growth. J Cell Sci 1996 109 467 477 The results of inhibition of MAP1B and Tau expression by antisense oligonucleotides suggests functional redundancy of the two proteins. 8838670
- Takei Y Teng J Harada A Hirokawa N Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J Cell Biol 2000 150 989 1000 This paper reports the crossing of MAP1B and Tau knockout animals; anatomical analysis shows defects in axon outgrowth and neuronal migration. 10973990 10.1083/jcb.150.5.989 PMC2175245 · DOI
- Teng J Takei Y Harada A Nakata T Chen J Hirokawa N Synergistic effects of MAP2 and MAP1B knockout in neuronal migration, dendritic outgrowth, and microtubule organization. J Cell Biol 2001 155 65 76 The first MAP2 knockout mouse is described. Crossing of MAP1B and MAP2 knockout animals leads to defects in dendrite outgrowth and neuronal migration. 11581286 10.1083/jcb.200106025 PMC2150794 · DOI
- Obar RA Dingus J Bayley H Vallee RB The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C. Neuron 1989 3 639 645 Mapping of the PKA-RII-binding domain on MAP2 is reported. 2561973 10.1016/0896-6273(89)90274-2 · DOI
- Gamblin TC Berry RW Binder LI Modeling tau polymerization in vitro: a review and synthesis. Biochemistry 2003 42 15009 15017 A review of biochemical analyses of Tau polymerization and its relevance for tauopathies. 14690409 10.1021/bi035722s · DOI
- Geschwind DH Tau phosphorylation, tangles, and neurodegeneration: the chicken or the egg? Neuron 2003 40 457 460 A review of the role of Tau phosphorylation in neurodegenerative diseases. 14642270 10.1016/S0896-6273(03)00681-0 · DOI
- Goedert M Ghetti B Spillantini MG Tau gene mutations in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Their relevance for understanding the neurogenerative process. Ann NY Acad Sci 2000 920 74 83 The role of Tau mutations in the specific tauopathy FTDP-17 is reviewed. 11193179
- Chapin SJ Bulinski JC Non-neuronal 210 × 10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of neuronal MAP2 and tau. J Cell Sci 1991 98 27 36 This paper reports the cloning of MAP4 and comparison of its sequence with MAP2 and Tau. 1905296
- Nguyen HL Chari S Gruber D Lue CM Chapin SJ Bulinski JC Overexpression of full- or partial-length MAP4 stabilizes microtubules and alters cell growth. J Cell Sci 1997 110 281 294 Stabilization of cellular microtubules by MAP4 is reported. 9044058
- Ookata K Hisanaga S Bulinski JC Murofushi H Aizawa H Itoh TJ Hotani H Okumura E Tachibana K Kishimoto T Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics. J Cell Biol 1995 128 849 862 This study reports an interaction of MAP4 with cyclin B and discusses its potential functional relevance for regulation of microtubules during mitosis. 7876309 10.1083/jcb.128.5.849 PMC2120387 · DOI
- Wang XM Peloquin JG Zhai Y Bulinski JC Borisy GG Removal of MAP4 from microtubules in vivo produces no observable phenotype at the cellular level. J Cell Biol 1996 132 345 357 In cultured cells, MAP4 was blocked using a function-blocking antibody. No phenotype was detected, suggesting that MAP4 is a component of a functionally redundant system. 8636213 10.1083/jcb.132.3.345 PMC2120719 · DOI
- Mangan ME Olmsted JB A muscle-specific variant of microtubule-associated protein 4 (MAP4) is required in myogene-sis. Development 1996 122 771 781 Defects in myogenesis in a muscle cell line lacking the muscle-specific MAP4 isoform were found. 8631255
- Papasozomenos SC Binder LI Microtubule-associated protein 2 (MAP2) is present in astrocytes of the optic nerve but absent from astrocytes of the optic tract. J Neurosci 1986 6 1748 1756 A report of the expression of MAP2 in specific astrocytes. 3712008 PMC6568727
- Vouyiouklis DA Brophy PJ Microtubule-associated proteins in developing oligodendrocytes: transient expression of a MAP2c isoform in oligodendrocyte precursors. J Neurosci Res 1995 42 803 817 The expression of the early neuronal MAP2 isoform MAP2c is analyzed during oligodendrocyte differentiation. 8847742
- Loveland KL Herszfeld D Chu B Rames E Christy E Briggs LJ Shakri R de Kretser DM Jans DA Novel low molecular weight microtubule-associated protein-2 isoforms contain a functional nuclear localization sequence. J Biol Chem 1999 274 19261 19268 The discovery of nuclear MAP2 isoforms containing an alternatively spliced nuclear localization sequence. 10383434 10.1074/jbc.274.27.19261 · DOI
- LoPresti P Szuchet S Papasozomenos SC Zinkowski RP Binder LI Functional implications for the microtubule-associated protein tau: localization in oligodendrocytes. Proc Natl Acad Sci USA 1995 92 10369 10373 Expression of Tau in oligodendrocytes. 7479786 PMC40798
- Muller R Heinrich M Heck S Blohm D Richter-Landsberg C Expression of microtubule-associated proteins MAP2 and tau in cultured rat brain oligodendrocytes. Cell Tissue Res 1997 288 239 249 Expression of both Tau and MAP2 was analyzed in oligodendrocytes and compared to neurons. 9082959 10.1007/s004410050809 · DOI · Paper page
- Klein C Kramer EM Cardine AM Schraven B Brandt R Trotter J Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. J Neurosci 2002 22 698 707 The role of an interaction between Fyn and Tau is analyzed. 11826099 PMC6758498
- Gamblin TC Nachmanoff K Halpain S Williams RCJ Recombinant microtubule-associated protein 2c reduces the dynamic instability of individual microtubules. Biochemistry 1996 35 12576 12586 A study of the effect of purified, recombinant MAP2c on microtubule dynamics in vitro. 8823195 10.1021/bi961135d · DOI
- Panda D Samuel JC Massie M Feinstein SC Wilson L Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease. Proc Natl Acad Sci USA 2003 100 9548 9553 The effects of different Tau isoforms on microtubule dynamics are reported and the relevance for neurodegenerative diseases is discussed. 12886013 10.1073/pnas.1633508100 PMC170955 · DOI · Paper page
- Ichihara K Kitazawa H Iguchi Y Hotani H Itoh TJ Visualization of the stop of microtubule depolymerization that occurs at the high-density region of microtubule-associated protein 2 (MAP2). J Mol Biol 2001 312 107 118 An analysis of the clustering of MAP2 on microtubules and its relevance for microtubule dynamics. 11545589 10.1006/jmbi.2001.4934 · DOI
- Kaech S Ludin B Matus A Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins. Neuron 1996 17 1189 1199 The short- and long-term dynamics of microtubules in the presence of MAP2 or Tau are characterized. 8982165 10.1016/S0896-6273(00)80249-4 · DOI
- Chen J Kanai Y Cowan NJ Hirokawa N Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons. Nature 1992 360 674 677 Characterization of the role of MAP2 and Tau projection domains in microtubule spacing in axons and dendrites. 1465130 10.1038/360674a0 · DOI · Paper page
- Kar S Fan J Smith MJ Goedert M Amos LA Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J 2003 22 70 77 A cryo-EM study that reports the binding of Tau to the inner surface of microtubules. 12505985 10.1093/emboj/cdg001 PMC140040 · DOI · Paper page
- Makrides V Massie MR Feinstein SC Lew J Evidence for two distinct binding sites for tau on microtubules. Proc Natl Acad Sci USA 2004 101 6746 6751 Tau binding to preassembled microtubules is compared to Tau binding after co-assembly with microtubules. The results suggest that Tau can bind microtubules in two distinct ways. 15096589 10.1073/pnas.0400992101 PMC404116 · DOI
- Trinczek B Ebneth A Mandelkow EM Mandelkow E Tau regulates the attachment/detachment but not the speed of motors in microtubule-dependent transport of single vesicles and organelles. J Cell Sci 1999 112 2355 2367 The effect of Tau on dynein- and kinesin-dependent cellular transport processes is reported. 10381391
- Ebneth A Godemann R Stamer K Illenberger S Trinczek B Mandelkow E Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J Cell Biol 1998 143 777 794 The effect of Tau overexpression on kinesin-dependent transport processes is reported. 9813097 10.1083/jcb.143.3.777 PMC2148132 · DOI · Paper page
- Hagiwara H Yorifuji H Sato-Yoshitake R Hirokawa N Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules. J Biol Chem 1994 269 3581 3589 A biochemical analysis of competition between MAPs and microtubule motors. 8106402
- Lopez LA Sheetz MP Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil Cytoskeleton 1993 24 1 16 The effect of MAP2 and Tau on dynein and kinesin activity is measured using microtubule sliding assays. 8319263
- Chang L Jones Y Ellisman MH Goldstein LS Karin M JNK1 is required for maintenance of neuronal microtubules and controls phosphorylation of microtubule-associated proteins. Dev Cell 2003 4 521 533 This report shows a reduced association of MAP2 with microtubules in Jnk1 knockout mice. 12689591 10.1016/S1534-5807(03)00094-7 · DOI
- Philpot BD Lim JH Halpain S Brunjes PC Experience-dependent modifications in MAP2 phosphorylation in rat olfactory bulb. J Neurosci 1997 17 9596 9604 A report of activity-dependent phosphorylation of a specific site on MAP2. 9391014 PMC6573422
- Cassimeris L Spittle C Regulation of microtubule-associated proteins. Int Rev Cytol 2001 210 163 226 This substantial review summarizes the activity and regulation of animal cell MAPs, including Tau and MAP2. 11580206
- Kim H Binder LI Rosenbaum JL The periodic association of MAP2 with brain microtubules in vitro. J Cell Biol 1979 80 266 276 A highly enriched MAP2 fraction was prepared from calf neurotubules and a MAP2-microtubule interaction and microtubule stabilization were found. 457745 10.1083/jcb.80.2.266 PMC2110341 · DOI
- Lim RWL Halpain S Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein. J Biol Chem 2000 275 20578 20587 A report of the interaction of MAP2 with Src and Grb2 and regulation of this interaction by Erk2. 10781592 10.1074/jbc.M001887200 · DOI
- Zamora-Leon SP Lee G Davies P Shafit-Zagardo B Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2. J Biol Chem 2001 276 39950 39958 A report of the interaction of Fyn with MAP2c and the regulation of this interaction by Erk2. 11546790 10.1074/jbc.M107807200 · DOI
- Leterrier JF Liem RK Shelanski ML Interactions between neurofilaments and microtubule-associated proteins: a possible mechanism for intraorganellar bridging. J Cell Biol 1982 95 982 986 An interaction of MAP2 with neurofilaments is reported. 6891384 10.1083/jcb.95.3.982 PMC2112930 · DOI
- Davare MA Dong F Rubin CS Hell JW The A-kinase anchor protein MAP2B and cAMP-dependent protein kinase are associated with class C L-type calcium channels in neurons. J Biol Chem 1999 274 30280 30287 This paper describes a role for MAP2 as an AKAP (A-kinase anchoring protein) for class C L-type calcium channels. 10514522 10.1074/jbc.274.42.30280 · DOI
- Rehbein M Kindler S Horke S Richter D Two trans-acting rat-brain proteins, MARTA1 and MARTA2, interact specifically with the dendritic targeting element in MAP2 mRNAs. Brain Res Mol Brain Res 2000 79 192 201 Two proteins were cloned that interact specifically with MAP2 mRNA elements responsible for dendritic targeting. 10925159 10.1016/S0169-328X(00)00114-5 · DOI
- Butner KA Kirschner MW Tau protein binds to microtubules through a flexible array of distributed weak sites. J Cell Biol 1991 115 717 730 Mapping of the microtubule binding site of Tau. 1918161 10.1083/jcb.115.3.717 PMC2289193 · DOI · Paper page
- Lee G Newman T Gard DL Band H Panchamoorthy G Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 1998 111 3167 3177 The interaction between Fyn and Tau is reported. 9763511
- Takashima A Murayama M Murayama O Kohno T Honda T Yasutake K Nihonmatsu N Mercken M Yamaguchi H Sugihara S Wolozin B Presenilin 1 associates with glycogen synthase kinase-3beta and its substrate tau. Proc Natl Acad Sci USA 1998 95 9637 9641 A report of the interaction of Presenilin 1 with GSK3-beta and Tau. 9689133 10.1073/pnas.95.16.9637 PMC21391 · DOI
- Strittmatter WJ Saunders AM Goedert M Weisgraber KH Dong LM Jakes R Huang DY Pericak-Vance M Schmechel D Roses AD Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease. Proc Natl Acad Sci USA 1994 91 11183 11186 A report of the interaction between ApoE and Tau. 7972031 PMC45191
- Baudier J Mochly-Rosen D Newton A Lee SH Koshland DE Jr Cole RD Comparison of S100b protein with calmodulin: interactions with melittin and microtubule-associated tau proteins and inhibition of phosphorylation of tau proteins by protein kinase C. Biochemistry 1987 26 2886 2893 The interaction between S100b and Tau is reported. 3111527
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Halpain, S., & Dehmelt, L. (2006) · Genome Biology · doi:10.1186/gb-2006-7-6-224 · Cited by 261 · see citing works
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Cobos, I., Borello, U., & Rubenstein, J. L. R. (2007) · Neuron · doi:10.1016/j.neuron.2007.05.024 · Cited by 246 · see citing works
Kinesin Assembly and Movement in Cells
Verhey, K. J., Kaul, N., & Soppina, V. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155310 · Cited by 231 · see citing works
Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains
Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222 · see citing works
The Role of the Microtubule Cytoskeleton in Neurodevelopmental Disorders
Lasser, M., Tiber, J., & Lowery, L. A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00165 · Cited by 201 · see citing works
Mechanisms of Taxane Resistance
Maloney, S., Spring, C., Morejon-Lasso, L., & Prosperi, J. (2020) · Cancers · doi:10.3390/cancers12113323 · Cited by 198 · see citing works
Cytoskeletal signaling: is memory encoded in microtubule lattices by CaMKII phosphorylation?
Craddock, T. J. A., Tuszynski, J. A., & Hameroff, S. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002421 · Cited by 160 · see citing works
Basheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159 · see citing works
Gupta, N., Ly, T., Zhang, Q., Kaufman, P. L., Weinreb, R. N., & Yücel, Y. H. (2007) · Experimental Eye Research · doi:10.1016/j.exer.2006.09.013 · Cited by 122 · see citing works
Rapamycin reverses status epilepticus-induced memory deficits and dendritic damage
Brewster, A. L., Lugo, J. N., Patil, V. V., Lee, W. L., Qian, Y., Vanegas, F., & Anderson, A. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057808 · Cited by 112 · see citing works
Edelbrock, A. N., Àlvarez, Z., Simkin, D., Fyrner, T., Chin, S. M., Sato, K., Kiskinis, E., & Stupp, S. I. (2018) · Nano Letters · doi:10.1021/acs.nanolett.8b02317 · Cited by 103 · see citing works
A Population Genetic Approach to Mapping Neurological Disorder Genes Using Deep Resequencing
Myers, R. A., Casals, F., Gauthier, J., Hamdan, F. F., Keebler, J., Boyko, A. R., Bustamante, C. D., Piton, A. M., Spiegelman, D., Henrion, E., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001318 · Cited by 97 · see citing works
Microtubule lattice spacing governs cohesive envelope formation of tau family proteins
Siahaan, V., Tan, R., Humhalova, T., Libusova, L., Lacey, S. E., Tan, T., Dacy, M., Ori-McKenney, K. M., McKenney, R. J., Braun, M., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01096-2 · Cited by 94 · see citing works
Deussing, J. M., Breu, J., Kuhne, C., Kallnik, M., Bunck, M., Glasl, L., Yen, Y.-C., Schmidt, M. V., Zurmuhlen, R., Vogl, A. M., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1049-10.2010 · Cited by 86 · see citing works
Sumigray, K. D., Foote, H. P., & Lechler, T. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201206143 · Cited by 77 · see citing works
Hwang, H.-W., Saito, Y., Park, C. Y., Blachère, N. E., Tajima, Y., Fak, J. J., Zucker-Scharff, I., & Darnell, R. B. (2017) · Neuron · doi:10.1016/j.neuron.2017.08.024 · Cited by 74 · see citing works
Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works
“It is widely believed that tau stabilises microtubules in the axon [9–12], and that disease-induced loss of tau from axonal microtubules leads to their destabilisation [13–15].”
BackgroundAnalysis of cytoskeletal and motility proteins in the sea urchin genome assembly
Morris, R. L., Hoffman, M. P., Obar, R. A., McCafferty, S. S., Gibbons, I. R., Leone, A. D., Cool, J., Allgood, E. L., Musante, A. M., Judkins, K. M., et al. (2006) · Developmental Biology · doi:10.1016/j.ydbio.2006.08.052 · Cited by 60 · see citing works
Roles of LIM kinases in central nervous system function and dysfunction
Cuberos, H., Vallée, B., Vourc'h, P., Tastet, J., Andres, C. R., & Bénédetti, H. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.032 · Cited by 54 · see citing works
Biological wires, communication systems, and implications for disease
Friesen, D. E., Craddock, T. J. A., Kalra, A. P., & Tuszynski, J. A. (2015) · Biosystems · doi:10.1016/j.biosystems.2014.10.006 · Cited by 48 · see citing works
Faulty splicing and cytoskeleton abnormalities in <scp>H</scp> untington's disease
Fernández‐Nogales, M., Santos‐Galindo, M., Hernández, I. H., Cabrera, J. R., & Lucas, J. J. (2016) · Brain Pathology · doi:10.1111/bpa.12430 · Cited by 41 · see citing works
p600/UBR4 in the central nervous system
Parsons, K., Nakatani, Y., & Nguyen, M. D. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1788-8 · Cited by 35 · see citing works
Immunolocalization of muscarinic M1 receptor in the rat medial prefrontal cortex
Oda, S., Tsuneoka, Y., Yoshida, S., Adachi‐Akahane, S., Ito, M., Kuroda, M., & Funato, H. (2018) · Journal of Comparative Neurology · doi:10.1002/cne.24409 · Cited by 27 · see citing works
Xie, C., Soeda, Y., Shinzaki, Y., In, Y., Tomoo, K., Ihara, Y., & Miyasaka, T. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13228 · Cited by 27 · see citing works
Mozzi, A., Forni, D., Cagliani, R., Pozzoli, U., Clerici, M., & Sironi, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-06440-4 · Cited by 19 · see citing works
MAP2 caps tau fibrils and inhibits aggregation
Holden, M. R., Krzesinski, B. J., Weismiller, H. A., Shady, J. R., & Margittai, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104891 · Cited by 13 · see citing works
Gąssowska-Dobrowolska, M., Czapski, G. A., Cieślik, M., Zajdel, K., Frontczak-Baniewicz, M., Babiec, L., & Adamczyk, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087303 · Cited by 10 · see citing works
Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons
Yonemura, Y., Sakai, Y., Nakata, R., Hagita-Tatsumoto, A., Miyasaka, T., & Misonou, H. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113407
- Authors
- Dehmelt
- Venue
- Genome biology
- Published
- 2004
- Volume
- 6
- Issue
- 1
- Pages
- 204
- ISSN
- 1465-6906 (ISSN-L)
- PMC
- PMC549057
- OpenAlex
- W2166555967
- Cited by
- 972
- References
- 5
- Citations by year
- 2026: 36 · 2025: 39 · 2024: 59 · 2023: 67 · 2022: 59 · 2021: 66 · 2020: 62 · 2019: 60 · 2018: 69 · 2017: 39 · 2016: 58 · 2015: 45 · 2014: 49 · 2013: 45 · 2012: 36
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Genome biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of Mental Health (R01MH050861)
- National Institute of Neurological Disorders and Stroke (R01NS037311)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- microtubule-associated proteins, MAP2, MAP4, tau protein, alternative splicing, microtubule-binding repeats, microtubule stabilization, actin binding, neurite initiation, Alzheimer's disease, mitogen-activated protein kinase, neurons
- MeSH terms
- Animals, Gene Expression Regulation, Microtubule-Associated Proteins, Neurons, tau Proteins, Evolution, Molecular
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