Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles

Prezel, Eléa; Elie, Auréliane; Delaroche, Julie; Stoppin‐Mellet, Virginie; Bosc, Christophe; Serre, Laurence; Fourest-Lieuvin, Anne; Andrieux, Annie; Vantard, Marylin; Arnal, Isabelle

doi:10.1091/mbc.e17-06-0429

Cited by 57 publications

(38 citation statements)

References 71 publications

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“…It was reported recently that the microtubule-binding protein Tau co-organizes microtubule and actin networks. 42,43 Dynamin 1 also could regulate both actin and microtubule dynamics to ensure proper podocyte function. Dynamin 1 and dynamin 2 might act coordinately to maintain the podocyte cytoskeletal structures, which is essential for their filtration function.…”

Section: Discussionmentioning

confidence: 99%

Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

Tachibana

Abe

et al. 2020

FASEB j.

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Section: Discussionmentioning

confidence: 99%

Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

Tachibana

Abe

et al. 2020

FASEB j.

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“…Tau binds tubulin via its microtubule-binding domains [141], with a single tau molecule crosslinking multiple tubulin dimers [6]. Original studies found that tau stabilises microtubules [62], reducing the frequency of catastrophes (sudden microtubule disintegration) [208]. Early studies found that tau reduces the concentration of tubulin required for polymerisation [276].…”

Section: Regulation Of Microtubules: the Primary Physiological Role Omentioning

confidence: 99%

The physiological roles of tau and Aβ: implications for Alzheimer’s disease pathology and therapeutics

2020

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Tau and amyloid beta (Aβ) are the prime suspects for driving pathology in Alzheimer’s disease (AD) and, as such, have become the focus of therapeutic development. Recent research, however, shows that these proteins have been highly conserved throughout evolution and may have crucial, physiological roles. Such functions may be lost during AD progression or be unintentionally disrupted by tau- or Aβ-targeting therapies. Tau has been revealed to be more than a simple stabiliser of microtubules, reported to play a role in a range of biological processes including myelination, glucose metabolism, axonal transport, microtubule dynamics, iron homeostasis, neurogenesis, motor function, learning and memory, neuronal excitability, and DNA protection. Aβ is similarly multifunctional, and is proposed to regulate learning and memory, angiogenesis, neurogenesis, repair leaks in the blood–brain barrier, promote recovery from injury, and act as an antimicrobial peptide and tumour suppressor. This review will discuss potential physiological roles of tau and Aβ, highlighting how changes to these functions may contribute to pathology, as well as the implications for therapeutic development. We propose that a balanced consideration of both the physiological and pathological roles of tau and Aβ will be essential for the design of safe and effective therapeutics.

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“…The functional and structural analogies between Tau and CC1 are further reflected in the fact that both Tau and CC1 are relevant for the organism to function during stress conditions; CC1 promotes cellulose synthesis during salt stress 5 , whereas Tau has emerged as a key regulator of stress-induced brain pathology in mice and oxidative stress in cultured fibroblasts 31,32 . Furthermore, similar to the tyrosine to alanine mutations in CC1, disease-related mutations in Tau cause distinct defects in microtubule organization 33 . While the typical PGGG-containing repeats of the Tau microtubule-binding domain (R1-R4) are not obvious from the CC1 sequence, the two proteins do contain four similarly spaced hydrophobic microtubule-binding regions (regions 1–4 in Fig.…”

Section: Discussionmentioning

confidence: 92%

A molecular mechanism for salt stress-induced microtubule array formation in Arabidopsis

Kesten

Wallmann

Schneider

et al. 2018

Preprint

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44Microtubules are filamentous structures necessary for cell division, motility and morphology, 45 with dynamics critically regulated by microtubule-associated proteins (MAPs). We outline 46 the molecular mechanism by which the MAP, COMPANION OF CELLULOSE 47 SYNTHASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth 48 under salt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules 49 at evenly distributed distances through four conserved hydrophobic regions. NMR analyses 50 revealed that two neighboring residues in the first hydrophobic binding motif are crucial for 51 the microtubule interaction, which we confirmed through live cell analyses. The microtubule-52 binding mechanism of CC1 is remarkably similar to that of the prominent neuropathology-53 related protein Tau, indicating evolutionary convergence of MAP functions across animal and 54 plant cells. 55 56 Introduction 57 Microtubules are tubular structures essential to morphogenesis, division and motility in 58 eukaryotic cells 1 . While animal cells typically contain a centrosome with radiating 59 microtubules toward the cell periphery, growing plant cells arrange their microtubules along 60 the cell cortex 2 . A major function of the cortical microtubules in plant cells is to direct the 61 synthesis of cellulose, a fundamental component of the cell wall essential to plant 62 morphology 3 . Cellulose is produced at the plasma membrane by Cellulose Synthase (CESA) 63 protein complexes (CSCs; 4 ) that display catalytically-driven motility along the membrane 3 . 64 The recently described microtubule-associated protein (MAP), Companion of Cellulose 65 Synthase1 (CC1), is an integral component of the CSC and sustains cellulose synthesis by 66promoting the formation of a stress-tolerant microtubule array during salt stress 5 . As 67 cellulose synthesis is key for plant growth, engineering of plants to better produce cellulose is 68 of utmost importance to agriculture. Indeed, understanding the molecular mechanism by 69 which CC1 controls cellulose synthesis may bear opportunities to improve cultivation on salt-70 affected lands. 71The microtubule network is highly dynamic, and its state is influenced by the action 72 of MAPs. The mammalian Tau/MAP2/MAP4 family represents the most investigated MAP 73 set, primarily due to Tau's importance in the pathology of neurodegenerative diseases 6-8 . In 74 vitro, Tau promotes polymerization and bundling of microtubules, and diffuses along the 75 microtubule lattice 9-11 . In the brain, Tau is predominantly located at the axons of neurons, 76 where it contributes to the microtubule organization that drives neurite outgrowth 12,13 . In 77 disease, Tau self-aggregates into neurofibrillary tangles that might trigger neurodegeneration 78 14 . Intriguingly, no clear homologs of the Tau/MAP2/MAP4 family have been identified in 79 plants 15,16 . Because the full scope of Tau's biological role remains elusive, identification of 80 Tau-related proteins outside the anima...

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Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles

Cited by 57 publications

References 71 publications

Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes

The physiological roles of tau and Aβ: implications for Alzheimer’s disease pathology and therapeutics

A molecular mechanism for salt stress-induced microtubule array formation in Arabidopsis

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