Extracting microtubule networks from superresolution single-molecule localization microscopy data

Zhang, Zhen; Nishimura, Yukako; Kanchanawong, Pakorn

doi:10.1091/mbc.e16-06-0421

Cited by 52 publications

(68 citation statements)

References 59 publications

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“…were processed as described previously 55 . The enhanced images were then 30 binarized to extract the microtubule traces by a threshold calculated using Otsu's method.…”

Section: Matrix Degradation Assaymentioning

confidence: 99%

A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions

et al. 2019

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“…were processed as described previously 55 . The enhanced images were then 30 binarized to extract the microtubule traces by a threshold calculated using Otsu's method.…”

Section: Matrix Degradation Assaymentioning

confidence: 99%

A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions

et al. 2019

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“…1A) or per area ( Fig. S1C) to reveal network complexity (Zhang et al, 2017) (see Materials and Methods). Reduced microtubule complexity was obvious in Arp2/3-inhibited cells, indicating that microtubule organization responded to branched actin alteration.…”

Section: Branched Actin Affects Microtubule Architecture Dynamics Anmentioning

confidence: 99%

“…The number of microtubule joints was analyzed per area or per cell. The number of joints was referred as microtubule complexity (Zhang et al, 2017).…”

Section: Microtubule Network Complexity Analysismentioning

confidence: 99%

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

Shi

Yuan

Huang

et al. 2019

Journal of Cell Science

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Actin and microtubule cytoskeletons regulate cell morphology, participate in organelle trafficking and function in response to diverse environmental cues. Precise spatial-temporal coordination between these two cytoskeletons is essential for cells to live and move. Here, we report a novel crosstalk between actin and microtubules, in which the branched actin maintains microtubule organization, dynamics and stability by affecting tubulin acetylation levels. We observed that acetylated tubulin significantly decreases upon perturbation of the Arp2/3-branched actin. We subsequently discover that HDAC6 participates in this process by altering its interaction with tubulin and the Arp2/3-stabilizer cortactin. We further identify that the homeostasis of branched actin controls mitochondrial distribution via this microtubule acetylation-dependent mechanism. Our findings shed new light on the integral view of cytoskeletal networks, highlighting post-translational modification as another possible form of cytoskeletal inter-regulation, aside from the established crosstalks through structural connection or upstream signaling pathways.

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“…To analyze microtubules, fluorescence images of MAP4-labeled microtubules were used 91 . The image processing was performed as described in 92 . The enhanced images were then binarized to extract the microtubule traces by a threshold calculated using Otsu's method.…”

Section: Image Processing and Data Analysismentioning

confidence: 99%

The cytoskeleton as a smart composite material: A unified pathway linking microtubules, myosin-II filaments and integrin adhesions

Rafiq

Nishimura

Plotnikov

et al. 2017

Preprint

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The role of microtubules in the mechanoregulation of integrin--mediated adhesions is poorly understood. Here, we show that uncoupling of microtubules from integrin adhesions by depletion or displacement of KANK family proteins connecting the adhesion protein talin with microtubule tips led to disruption of podosomes and augmentation of focal adhesions, similarly to total disruption of microtubules. Using structured--illumination microscopy, we demonstrate that microtubule uncoupling from adhesions or total microtubule disruption brings about a massive assembly of myosin--IIA filaments, whilst a burst of microtubule polymerization led to a transient disassembly of myosin--IIA filaments. We showed that myosin--IIA filaments are indispensable for microtubule--dependent regulation of focal adhesions and podosomes. The microtubule--driven control of myosin--IIA filament formation is achieved through the regulation of Rho by microtubule--localized Rho guanine nucleotide exchange factor GEF--H1. Thus, a unifying mechanism of microtubule--mediated regulation of focal adhesions and podosomes operates via KANKs--and GEF--H1--dependent local reorganization of myosin--II filaments.All rights reserved. No reuse allowed without permission.(which was not peer-reviewed) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.

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Extracting microtubule networks from superresolution single-molecule localization microscopy data

Cited by 52 publications

References 59 publications

A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions

A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions

Arp2/3-branched actin regulates microtubule acetylation levels and affects mitochondrial distribution

The cytoskeleton as a smart composite material: A unified pathway linking microtubules, myosin-II filaments and integrin adhesions

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