The tau proteins in neuronal growth and development

Brandt, Roland

doi:10.2741/a120

Cited by 40 publications

(31 citation statements)

References 112 publications

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“…Tau regulates the assembly and stability of microtubules in neurons (for review, see Brandt, 1996). In the Taiep mutant rat, the polarized orientation of microtubules (Lunn et al, 1997) is abnormal, and Tau protein accumulates in the cell body and processes of oligodendrocytes, resulting in an intracellular accumulation of myelin proteins, hypomyelination, and progressive demyelination (Song et al, 2001a,b).…”

Section: Overexpression Of a Tau Deletion Mutant Inhibits Oligodendromentioning

confidence: 99%

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Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau

Klein¹,

Krämer²,

et al. 2002

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Fyn kinase plays an important role during myelination and has been shown to promote morphological differentiation of cultured oligodendrocytes. We analyzed the downstream targets of Fyn kinase in oligodendrocytes. Because process outgrowth and wrapping of axons involve cytoskeletal rearrangement, we focused on cytoskeletal proteins linked to Fyn. Here we demonstrate that Fyn binds to the cytoskeletal proteins Tau and ␣-Tubulin in oligodendrocytes. Tau interacts with the Fyn SH3 domain whereas ␣-Tubulin binds to the Fyn SH2 and SH3 domains. To study the function of the Fyn-Tau interaction in oligodendrocytes, we designed a Tau deletion mutant that would compete with endogenous Tau-Fyn binding in transfected cells. The mutant Tau protein binds to the Fyn SH3 domain but lacks the microtubuli interaction domain and thus cannot bind to microtubuli. In the presence of the mutant Tau protein, a reduction of the process number and process length in oligodendroglial cells was observed. This effect is likely to be caused by interference with the Fyn-Tau-microtubuli cascade rather than inactivation of the kinase, because Fyn bound to the mutant Tau retains activity. A similar inhibition of process outgrowth was observed when oliogodendroglial cells were cultured in the presence of Fumonisin B1, an inhibitor of sphingolipid synthesis that prevents the formation of rafts. Because ligation of the cell adhesion molecule F3 on oligodendrocytes leads to activation of Fyn kinase localized in rafts, these findings suggest that recruitment of Tau and Tubulin to activated Fyn kinase in rafts is an important step in the initiation of myelination. Key words: myelination; oligodendrocytes; Fyn kinase; cytoskeleton; Tau; glycosphingolipid-rich raftsThe myelination of axons by oligodendrocytes involves the coordinated recognition of the axonal surface, ensheathment of the axonal process, and ultimately compaction of the wrappings of oligodendroglial membrane to generate the myelin sheath. The interplay of the adhesion molecules expressed by oligodendrocytes and axons as well as the downstream signal transduction cascades mediating these complex cellular interactions still remain primarily unelucidated (Pedraza et al., 2001).Substantial evidence exists that Fyn expressed by oligodendrocytes plays an important role in myelination. Mice deficient for Fyn kinase are hypomyelinated (Umemori et al., 1994;). In addition, knock-in mice expressing a kinase-defective Fyn protein that cannot be activated because of a mutation in the ATP-binding site of Fyn show severe myelination defects . Inhibition of the Fyn activity in cultured oligodendrocytes using kinase inhibitors or dominant negative Fyn constructs inhibited the process outgrowth of the cells (Osterhout et al., 1999). We have shown that in oligodendrocytes [as in neurons (Zisch et al., 1995)] the F3 adhesion molecule is complexed to the Src-family tyrosine kinase Fyn and that this association takes place within glycosphingolipid (gsl)/cholesterol-rich microdomains (Kramer et al., 1999), ge...

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Section: Overexpression Of a Tau Deletion Mutant Inhibits Oligodendromentioning

confidence: 99%

“…Tau induces microtubule assembly and bundle formation leading to process formation (for review, see Brandt, 1996). In a neuroblastoma cell line, Tau has been shown to associate with the Fyn SH3 domain (Lee et al, 1998).…”

Section: Abstract: Myelination; Oligodendrocytes; Fyn Kinase; Cytoskmentioning

confidence: 99%

Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau

Klein¹,

Krämer²,

et al. 2002

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“…Within this context, another aspect to emphasize in the analysis of cellular factors affecting the extension of neurites by neuronal cells is the role of tau in mediating microtubule-actin filament interactions (5,10,24), an activity that could be involved in regulating the actin cortex and association with plasma membrane in the establishment of architectural patterns during neuronal growth (25).…”

Section: The Role Of Tau In Neuronal Growthmentioning

confidence: 99%

Regulatory roles of microtubule-associated proteins in neuronal morphogenesis. Involvement of the extracellular matrix

Ramı́rez

Álvarez

Garcia-Abreu

et al. 1999

Braz J Med Biol Res

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As a result of recent investigations, the cytoskeleton can be viewed as a cytoplasmic system of interconnected filaments with three major integrative levels: self-assembling macromolecules, filamentous polymers, e.g., microtubules, intermediate filaments and actin filaments, and supramolecular structures formed by bundles of these filaments or networks resulting from cross-bridges between these major cytoskeletal polymers. The organization of this biological structure appears to be sensitive to fine spatially and temporally dependent regulatory signals. In differentiating neurons, regulation of cytoskeleton organization is particularly relevant, and the microtubule-associated protein (MAP) tau appears to play roles in the extension of large neuritic processes and axons as well as in the stabilization of microtubular polymers along these processes. Within this context, tau is directly involved in defining neuronal polarity as well as in the generation of neuronal growth cones. There is increasing evidence that elements of the extracellular matrix contribute to the control of cytoskeleton organization in differentiating neurons, and that these regulations could be mediated by changes in MAP activity. In this brief review, we discuss the possible roles of tau in mediating the effects of extracellular matrix components on the internal cytoskeletal arrays and its organization in growing neurons.

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“…In microtubule assembly, tau participates in the nucleation of tubulin. Tau also modulates the dynamic instability of tubulin assembly by affecting the rates of polymerization, and the proper formation of microtubules (Brandt, 1996;Weingarten et al, 1975). Phosphorylation of tau protein is developmentally regulated.…”

Section: Introductionmentioning

confidence: 99%

“…The MAP protein tau found mainly in mammalian neuronal cells is a hydrophilic, phosphoprotein, that is reported to play a major role in microtubule assembly, stabilization and bundling (Brandt, 1996;Oyama et al, 2004). Tau is coded for by a single gene located on chromosome 17.…”

Section: Introductionmentioning

confidence: 99%

Expression of neuronal protein Tau in Candida albicans

Manen¹,

Guariglia²,

Alonso³

et al. 2014

J. Yeast Fungal Res.

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Candida albicans is a dimorphic, opportunist fungal pathogen in which cell adhesion and filamentation contribute to host tissue invasiveness and fungal pathogenicity. Morphogenesis in C. albicans which involves yeast to hyphae transition is dependent on temperature, the growth media composition, and is regulated by quorum sensing. In yeasts, filament formation and polarized growth are associated with the actin cytoskeletal network and microtubule interactions. The microtubule associated protein (MAP), Tau (tau), is a neuronal protein in mammals that participates in microtubule binding, microtubule assembly, bundling and stabilization. In the current study, we generated an electroporated tau derivative of a strain of C. albicans. We have observed that tau expression accelerates and increases the extent of medium dependent filamentation. We have also noted tau interacts mainly with actin filaments and to some extent, microtubules. We believe that these interactions are involved in the temporal control of filament formation in tau-containing cells.

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The tau proteins in neuronal growth and development

Cited by 40 publications

References 112 publications

Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau

Process Outgrowth of Oligodendrocytes Is Promoted by Interaction of Fyn Kinase with the Cytoskeletal Protein Tau

Regulatory roles of microtubule-associated proteins in neuronal morphogenesis. Involvement of the extracellular matrix

Expression of neuronal protein Tau in Candida albicans

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