Interaction between microtubule-associated protein tau and spectrin

Carlier, Marie‐France; Simon, C.; Cassoly, Robert; Pradel, Louise‐Anne

doi:10.1016/0300-9084(84)90007-5

Cited by 56 publications

(28 citation statements)

References 30 publications

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“…It is possible that this component is part of such a microtubule-tau-plasma membrane complex. In vitro, tau interacts with spectrin (96), which may provide another link to the membrane skeleton. One may speculate that tau has a role in maintaining the axonspecific plasma membrane composition by anchoring the components of plasma membranes to the microtubule system (Figure 7).…”

Section: A Role For Tau Beyond Promoting Microtubule Assemblymentioning

confidence: 99%

The tau proteins in neuronal growth and development

Brandt¹

1996

Front Biosci

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The neuronal microtubule-associated protein tau has been implicated as having a role in the outgrowth of neural processes and the development of neuronal polarity. In vitro, tau promotes microtubule assembly, stabilizes cellular microtubules, and affects their dynamic behavior. Antisense experiments using cultured neurons provided evidence for an essential role of tau in the development of axons. However, tau knockout mice turned out to be surprisingly healthy and developed neurons which were functionally and structurally almost normal. This raises the question of how essential tau is for neuronal development. In the first part of this paper, data on the function of tau as a microtubule assembly-promoting and stabilizing factor are reviewed. Then, studies investigating the role of tau in the development of neuronal polarity are discussed. In the last part, recent results which provide evidence for a role of tau not directly related to its activity on microtubule assembly are summarized. INTRODUCTIONNeurons are one of the most extreme cell types in that they contain processes which can reach a meter or longer and encompass more than 99% of the cellular volume. This requires the presence of a sophisticated molecular machinery in order to establish and maintain such a morphology. From

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Section: A Role For Tau Beyond Promoting Microtubule Assemblymentioning

confidence: 99%

The tau proteins in neuronal growth and development

Brandt¹

1996

Front Biosci

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“…Major differences between the erythroid model and other cells include differences in the expression of spectrin (8 -11) and ankyrin isoforms (12)(13)(14)(15) (reviewed in Ref. 16), interactions of spectrin and ankyrin with additional proteins (17)(18)(19)(20)(21), localization of spectrin in the cytoplasm as well as in the plasma membrane (10,11,22), and the potential for dramatic rearrangements of spectrin's cellular location (23,24) (reviewed in Refs. 2 …”

Section: From the New York State Institute For Basic Research In Devementioning

confidence: 99%

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Ziemnicka-Kotula

et al. 1998

Journal of Biological Chemistry

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Erythroid spectrin is the predominant component of the twodimensional protein network called the membrane skeleton, underlying the lipid bilayer of red cells (for recent reviews, seeRefs. 1-3). Formation of the membrane skeleton involves multiple protein-protein interactions among integral membrane proteins. Interactions of spectrin with other membrane proteins such as ankyrin, protein 4.1, and adducin provide a linkage of spectrin either to the plasma membrane or among spectrin tetramers. Many hereditary anemia mutations affect interactions of these integral membrane proteins, resulting in increased fragility and shortened lifespan of erythrocytes. In hereditary elliptocytosis and pyropoikilocytosis, the mutations have been localized in the ␣-and ␤-subunits of spectrin (reviewed in Refs. 4 and 5). Many of these proteins, including spectrin, which were first identified in red cells, have isoforms expressed in nonerythroid cells, but the structure and regulatory processes of the nonerythroid membrane skeleton are less well understood (reviewed in Refs. 1-3, 6, and 7). Functional differences between the membranes of erythroid and nonerythroid cells argue against the simple erythrocyte model of the membrane skeleton. Major differences between the erythroid model and other cells include differences in the expression of spectrin (8 -11) and ankyrin isoforms (12-15) (reviewed in Ref.16), interactions of spectrin and ankyrin with additional proteins (17-21), localization of spectrin in the cytoplasm as well as in the plasma membrane (10,11,22), and the potential for dramatic rearrangements of spectrin's cellular location (23, 24) (reviewed in Refs. 2 and 7).Several studies have demonstrated that both erythroid and nonerythroid spectrins are expressed in brain tissue (8 -11, 25). Neuronal compartmentalization of brain spectrin isoforms into axons and presynaptic terminals (nonerythroid spectrin) and into cell bodies and dendrites (erythroid spectrin) (10, 25) suggests that brain spectrin isoforms may perform related but distinct functions in neuronal cells. It has been suggested that nonerythroid spectrin performs a more general, constitutive role, while erythroid spectrin takes part in more specialized activities of differentiated cells (26). The ␣-subunit of erythroid spectrin, ␣I (27), 1 and the ␣-subunit of nonerythroid spectrin, ␣II (28, 29), each contains a unique SH3 2 domain. Distinct protein interactions are likely to involve these domains, and they may be important for specific distribution and specialized roles of brain spectrin isoforms.

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“…Tau also interacts with the neuronal plasma membrane and anchors enzymes to MTs (Brandt et al 1995;Lee et al 1998;Sontag et al 1999). Tau can also associate with spectrin (Carlier et al 1984), actin (Griffith and Pollard 1982), PP1 and PP2A Sontag et al 1999), kinases like CDK5 (Sobue et al 2000), presenilin 1 (Takashima et al 1998), α-synuclein (Jensen et al 1999), phospholipase C (Hwang et al 1996), the Fyn tyrosine kinase (Klein et al 2002;Lee et al 1998), apolipoprotein E (Strittmatter et al 1994), and calmodulin (Baudier et al 1987). It can also bind to chaperones such as Hsp70, Hsp90, and Pin-1 (Dou et al 2003;Lu et al 1999).…”

Section: Tau/mapt Family Of Microtubule-associated Proteinsmentioning

confidence: 99%

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

2016

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Dendrites have a unique microtubule organization. In vertebrates, dendritic microtubules are organized in antiparallel bundles, oriented with their plus ends either pointing away or toward the soma. The mixed microtubule arrays control intracellular trafficking and local signaling pathways, and are essential for dendrite development and function. The organization of microtubule arrays largely depends on the combined function of different microtubule regulatory factors or generally named microtubule-associated proteins (MAPs). Classical MAPs, also called structural MAPs, were identified more than 20 years ago based on their ability to bind to and copurify with microtubules. Most classical MAPs bind along the microtubule lattice and regulate microtubule polymerization, bundling, and stabilization. Recent evidences suggest that classical MAPs also guide motor protein transport, interact with the actin cytoskeleton, and act in various neuronal signaling networks. Here, we give an overview of microtubule organization in dendrites and the role of classical MAPs in dendrite development, dendritic spine formation, and synaptic plasticity. IntroductionMicrotubules (MTs) are cytoskeletal structures that play essential roles in all eukaryotic cells. MTs are important not only during cell division but also in non-dividing cells, where they are critical structures in numerous cellular processes such as cell motility, migration, differentiation, intracellular transport and organelle positioning. MTs are composed of two proteins, α-and β-tubulin, that form heterodimers and organize themselves in a head-to-tail manner. MTs are dynamic and they can rapidly switch between cycles of growth and shrinkage. This MT

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Interaction between microtubule-associated protein tau and spectrin

Cited by 56 publications

References 30 publications

The tau proteins in neuronal growth and development

The tau proteins in neuronal growth and development

Identification of a Candidate Human Spectrin Src Homology 3 Domain-binding Protein Suggests a General Mechanism of Association of Tyrosine Kinases with the Spectrin-based Membrane Skeleton

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

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