The Molecular and Cellular Biology of Tau

Tau protein was a well‐studied molecule before it was discovered in the Alzheimer neurofibrillary tangles. As a microtubule‐associated protein (MAP), it continues to be of interest to microtubule biologists who have provided a rather rich knowledge about this protein. Recent work suggests that tau, a neuronal MAR is capable of generating some features of an axonal shape and an axon‐like organization of the cytoskeleton. The importance of tau in pathology stems from its relationship to Alzheimer paired helical filaments and dystrophic neurites. Tau was first believed to be a component of paired helical filaments based upon immunocytochemical grounds (1–6) and then conclusively demonstrated by protein chemical techniques (7–9). Most recently it was shown that bacterially expressed tau fragments from the microtubule‐binding domain can self‐assemble into paired helical filaments that resemble those from the Alzheimer brain (10).

[1]  R. Braun,et al.  Proline-directed phosphorylation of human Tau protein. , 1992, The Journal of biological chemistry.

[2]  J. Wood,et al.  Differential sensitivity of the microtubule-associated protein, tau, in Alzheimer's disease tissue to formalin fixation. , 1988, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[3]  K. Kosik,et al.  Axonal disruption and aberrant localization of tau protein characterize the neuropil pathology of Alzheimer's disease , 1987, Annals of neurology.

[4]  K. Kosik,et al.  Overexpression of tau in a nonneuronal cell induces long cellular processes , 1991, The Journal of cell biology.

[5]  K. Imahori,et al.  Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. , 1992, The Journal of biological chemistry.

[6]  G. Drewes,et al.  Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro , 1992, The Journal of cell biology.

[7]  K. Imahori,et al.  A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope , 1991, Neuroscience Letters.

[8]  S. Moreno,et al.  Substrates for p34 cdc2 : In vivo veritas? , 1990, Cell.

[9]  R. Neve,et al.  Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. , 1986, Brain research.

[10]  A. Delacourte,et al.  Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments , 1986, Journal of the Neurological Sciences.

[11]  D. Selkoe,et al.  Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[12]  A. Frankfurter,et al.  The distribution of tau in the mammalian central nervous system , 1985, The Journal of cell biology.

[13]  G. Innocenti,et al.  Differential Distribution of Tau Proteins in Developing Cat Cerebral Cortex and Corpus Callosum , 1991, The European journal of neuroscience.

[14]  L. Binder,et al.  Phosphorylation determines two distinct species of Tau in the central nervous system. , 1987, Cell motility and the cytoskeleton.

[15]  R. Crowther,et al.  Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain. , 1989, The EMBO journal.

[16]  J L Haines,et al.  A genetic linkage map of chromosome 17. , 1990, Genomics.

[17]  K. Imahori,et al.  A novel tubulin-dependent protein kinase forming a paired helical filament epitope on tau. , 1988, Journal of biochemistry.

[18]  H. Kawasaki,et al.  A common amino acid sequence in 190-kDa microtubule-associated protein and tau for the promotion of microtubule assembly. , 1989, The Journal of biological chemistry.

[19]  M. Kirschner,et al.  Tau protein binds to microtubules through a flexible array of distributed weak sites , 1991, The Journal of cell biology.

[20]  K. Kosik,et al.  Processes induced by tau expression in Sf9 cells have an axon-like microtubule organization , 1991, The Journal of cell biology.

[21]  K. Kosik,et al.  The effect of tau antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons , 1991, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[22]  L. Binder,et al.  Biochemical and immunological analyses of cytoskeletal domains of neurons , 1986, The Journal of cell biology.

[23]  M. Kirschner,et al.  The primary structure and heterogeneity of tau protein from mouse brain. , 1988, Science.

[24]  J. Brion,et al.  Both adult and juvenile tau microtubule-associated proteins are axon specific in the developing and adult rat cerebellum , 1988, Neuroscience.

[25]  R. Liem,et al.  Two separate 18-amino acid domains of tau promote the polymerization of tubulin. , 1989, The Journal of biological chemistry.

[26]  H. Wiśniewski,et al.  Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. , 1986, The Journal of biological chemistry.

[27]  M. Kirschner,et al.  Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. , 1977, Journal of molecular biology.

[28]  A. Klug,et al.  Structural characterization of the core of the paired helical filament of Alzheimer disease. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[29]  S. Pelech,et al.  Mitogen-activated protein kinases: versatile transducers for cell signaling. , 1992, Trends in biochemical sciences.

[30]  A. Himmler.  Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family , 1989, Molecular and cellular biology.

[31]  K. Kosik,et al.  Structure and novel exons of the human tau gene. , 1992, Biochemistry.

[32]  S. Mirra,et al.  Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau) , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[33]  Y. Ihara,et al.  One of the antigenic determinants of paired helical filaments is related to tau protein. , 1986, Journal of biochemistry.

[34]  E. Mandelkow,et al.  Structure and elasticity of microtubule-associated protein tau , 1988, Nature.

[35]  K. Kosik,et al.  Microtubule destabilization and neurofilament phosphorylation precede dendritic sprouting after close axotomy of lamprey central neurons. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[36]  Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau) , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[37]  J. Olmsted,et al.  A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences. , 1991, The Journal of biological chemistry.

[38]  K. Kosik,et al.  Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons , 1990, Nature.

[39]  N. Hirokawa,et al.  Tau Proteins: the Molecular Structure and Mode of Binding on Microtubules Materials and Methods Isolation of Tau , 1988 .

[40]  S. Lewis,et al.  Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein , 1988, Science.

[41]  K. Titani,et al.  Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. , 1992, The Journal of biological chemistry.

[42]  N. Cairns,et al.  Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms , 1992, Neuron.

[43]  M. Kirschner,et al.  Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains , 1989, Molecular and cellular biology.

[44]  E. Mandelkow,et al.  Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation , 1989, The Journal of cell biology.

[45]  R. Neve,et al.  Tau in situ hybridization in normal and alzheimer brain: Localization in the somatodendritic compartment , 1989, Annals of neurology.

[46]  M. Shelanski,et al.  Light and electron microscope localization of the microtubule- associated tau protein in rat brain , 1988, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[47]  J. Joly,et al.  Peptides corresponding to the second repeated sequence in MAP-2 inhibit binding of microtubule-associated proteins to microtubules. , 1990, Biochemistry.

[48]  R. Neve,et al.  The microtubule binding domain of tau protein , 1989, Neuron.

[49]  E. Masliah,et al.  Alz-50 recognizes a phosphorylated epitope of tau protein , 1990, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[50]  HM Roder,et al.  Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios , 1991, The Journal of neuroscience : the official journal of the Society for Neuroscience.

[51]  J. Walker,et al.  Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[52]  E. Mandelkow,et al.  The Alzheimer‐like phosphorylation of tau protein reduces microtubule binding and involves Ser‐Pro and Thr‐Pro motifs , 1992, FEBS letters.

[53]  M. Kirschner,et al.  Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. , 1977, Journal of molecular biology.

[54]  Kenneth S. Kosik,et al.  Developmentally regulated expression of specific tau sequences , 1989, Neuron.

[55]  K. Kosik,et al.  Suppression of MAP2 in cultured cerebeller macroneurons inhibits minor neurite formation , 1992, Neuron.

[56]  R. Liem,et al.  Primary structure of high molecular weight tau present in the peripheral nervous system. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[57]  J. Bulinski,et al.  Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4) contains a domain homologous to the microtubule-binding domains of neuronal MAP2 and tau. , 1991, Journal of cell science.