Shaping microtubules into diverse patterns: Molecular connections for setting up both ends

Mimori-Kiyosue, Yuko

doi:10.1002/cm.20540

Cited by 42 publications

(43 citation statements)

References 183 publications

(117 reference statements)

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“…Given the great number of proteins involved in both positively and negatively regulating MT assembly and disassembly (Mimori-Kiyosue, 2011), our results support the hypothesis that an optimal level of MT stability is required for proper neuronal morphogenesis. The finding that negative regulators of MT stability, such as the α-tubulin isotype TBA-7 and the MT-destabilizing kinesin-13 KLP-7, prevent excessive TRN neurite growth further supports this hypothesis.…”

Section: Discussionsupporting

confidence: 79%

Distinct effects of tubulin isotype mutations on neurite growth inCaenorhabditis elegans

Zheng

Diaz‐Cuadros

Nguyen

et al. 2017

MBoC

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Section: Discussionsupporting

confidence: 79%

Distinct effects of tubulin isotype mutations on neurite growth inCaenorhabditis elegans

Zheng

Diaz‐Cuadros

Nguyen

et al. 2017

MBoC

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“…Although many proteins that modulate plus-end dynamics have been identified (7), how the minus-ends are controlled at noncentrosomal sites remains less well understood (2,(8)(9)(10). CAMSAP3 (also known as Nezha) is a member of the calmodulin-regulatedspectrin-associated proteins (CAMSAP)/Nezha/Patronin family proteins, which bind and stabilize the minus-ends of microtubules (11)(12)(13)(14)(15)(16)(17)(18).…”

mentioning

confidence: 99%

CAMSAP3 orients the apical-to-basal polarity of microtubule arrays in epithelial cells

Toya¹,

Kobayashi²,

Kawasaki³

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

127

171

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Polarized epithelial cells exhibit a characteristic array of microtubules that are oriented along the apicobasal axis of the cells. The minus-ends of these microtubules face apically, and the plus-ends face toward the basal side. The mechanisms underlying this epithelial-specific microtubule assembly remain unresolved, however. Here, using mouse intestinal cells and human Caco-2 cells, we show that the microtubule minus-end binding protein CAMSAP3 (calmodulin-regulated–spectrin-associated protein 3) plays a pivotal role in orienting the apical-to-basal polarity of microtubules in epithelial cells. In these cells, CAMSAP3 accumulated at the apical cortices, and tethered the longitudinal microtubules to these sites. Camsap3 mutation or depletion resulted in a random orientation of these microtubules; concomitantly, the stereotypic positioning of the nucleus and Golgi apparatus was perturbed. In contrast, the integrity of the plasma membrane was hardly affected, although its structural stability was decreased. Further analysis revealed that the CC1 domain of CAMSAP3 is crucial for its apical localization, and that forced mislocalization of CAMSAP3 disturbs the epithelial architecture. These findings demonstrate that apically localized CAMSAP3 determines the proper orientation of microtubules, and in turn that of organelles, in mature mammalian epithelial cells.

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“…Aligned MTs are a hallmark of specialized cell types with non-centrosomal MTs, such as neuronal and epithelial cells12. The MT alignment creates a structural scaffold for vectorial transport of different cargos, and therefore plays important functions in cell polarity, cell shape and cell migration3.…”

mentioning

confidence: 99%

Microtubule organization is determined by the shape of epithelial cells

et al. 2016

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Interphase microtubule organization is critical for cell function and tissue architecture. In general, physical mechanisms are sufficient to drive microtubule organization in single cells, whereas cells within tissues are thought to utilize signalling mechanisms. By improving the imaging and quantitation of microtubule alignment within developing Drosophila embryos, here we demonstrate that microtubule alignment underneath the apical surface of epithelial cells follows cell shape. During development, epidermal cell elongation and microtubule alignment occur simultaneously, but by perturbing cell shape, we discover that microtubule organization responds to cell shape, rather than the converse. A simple set of microtubule behaviour rules is sufficient for a computer model to mimic the observed responses to changes in cell surface geometry. Moreover, we show that microtubules colliding with cell boundaries zip-up or depolymerize in an angle-dependent manner, as predicted by the model. Finally, we show microtubule alignment responds to cell shape in diverse epithelia.

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Shaping microtubules into diverse patterns: Molecular connections for setting up both ends

Cited by 42 publications

References 183 publications

Distinct effects of tubulin isotype mutations on neurite growth inCaenorhabditis elegans

Distinct effects of tubulin isotype mutations on neurite growth inCaenorhabditis elegans

CAMSAP3 orients the apical-to-basal polarity of microtubule arrays in epithelial cells

Microtubule organization is determined by the shape of epithelial cells

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