Resolving bundled microtubules using anti-tubulin nanobodies

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Resolving bundled microtubules using anti-tubulin nanobodies. / Mikhaylova, Marina; Cloin, Bas M.C.; Finan, Kieran; van den Berg, Robert; Teeuw, Jalmar; Kijanka, Marta M.; Sokolowski, Mikolaj; Katrukha, Eugene A.; Maidorn, Manuel; Opazo, Felipe; Moutel, Sandrine; Vantard, Marilyn; Perez, Frank; van Bergen en Henegouwen, Paul M. P.; Hoogenraad, Casper C.; Ewers, Helge; Kapitein, Lukas C.

In: NAT COMMUN, Vol. 6, No. 7933, 11.08.2015.

Research output: SCORING: Contribution to journalSCORING: Journal articleResearchpeer-review

Harvard

Mikhaylova, M, Cloin, BMC, Finan, K, van den Berg, R, Teeuw, J, Kijanka, MM, Sokolowski, M, Katrukha, EA, Maidorn, M, Opazo, F, Moutel, S, Vantard, M, Perez, F, van Bergen en Henegouwen, PMP, Hoogenraad, CC, Ewers, H & Kapitein, LC 2015, 'Resolving bundled microtubules using anti-tubulin nanobodies', NAT COMMUN, vol. 6, no. 7933. https://doi.org/doi: 10.1038/ncomms8933

APA

Mikhaylova, M., Cloin, B. M. C., Finan, K., van den Berg, R., Teeuw, J., Kijanka, M. M., Sokolowski, M., Katrukha, E. A., Maidorn, M., Opazo, F., Moutel, S., Vantard, M., Perez, F., van Bergen en Henegouwen, P. M. P., Hoogenraad, C. C., Ewers, H., & Kapitein, L. C. (2015). Resolving bundled microtubules using anti-tubulin nanobodies. NAT COMMUN, 6(7933). https://doi.org/doi: 10.1038/ncomms8933

Vancouver

Mikhaylova M, Cloin BMC, Finan K, van den Berg R, Teeuw J, Kijanka MM et al. Resolving bundled microtubules using anti-tubulin nanobodies. NAT COMMUN. 2015 Aug 11;6(7933). https://doi.org/doi: 10.1038/ncomms8933

Bibtex

@article{81215f20d1b04834a790e7ea20bfd4fe,
title = "Resolving bundled microtubules using anti-tubulin nanobodies",
abstract = "Microtubules are hollow biopolymers of 25-nm diameter and are key constituents of the cytoskeleton. In neurons, microtubules are organized differently between axons and dendrites, but their precise organization in different compartments is not completely understood. Super-resolution microscopy techniques can detect specific structures at an increased resolution, but the narrow spacing between neuronal microtubules poses challenges because most existing labelling strategies increase the effective microtubule diameter by 20-40 nm and will thereby blend neighbouring microtubules into one structure. Here we develop single-chain antibody fragments (nanobodies) against tubulin to achieve super-resolution imaging of microtubules with a decreased apparent diameter. To test the resolving power of these novel probes, we generate microtubule bundles with a known spacing of 50-70 nm and successfully resolve individual microtubules. Individual bundled microtubules can also be resolved in different mammalian cells, including hippocampal neurons, allowing novel insights into fundamental mechanisms of microtubule organization in cell- and neurobiology. ",
author = "Marina Mikhaylova and Cloin, {Bas M.C.} and Kieran Finan and {van den Berg}, Robert and Jalmar Teeuw and Kijanka, {Marta M.} and Mikolaj Sokolowski and Katrukha, {Eugene A.} and Manuel Maidorn and Felipe Opazo and Sandrine Moutel and Marilyn Vantard and Frank Perez and {van Bergen en Henegouwen}, {Paul M. P.} and Hoogenraad, {Casper C.} and Helge Ewers and Kapitein, {Lukas C.}",
year = "2015",
month = aug,
day = "11",
doi = "doi: 10.1038/ncomms8933",
language = "English",
volume = "6",
journal = "NAT COMMUN",
issn = "2041-1723",
publisher = "NATURE PUBLISHING GROUP",
number = "7933",

}

RIS

TY - JOUR

T1 - Resolving bundled microtubules using anti-tubulin nanobodies

AU - Mikhaylova, Marina

AU - Cloin, Bas M.C.

AU - Finan, Kieran

AU - van den Berg, Robert

AU - Teeuw, Jalmar

AU - Kijanka, Marta M.

AU - Sokolowski, Mikolaj

AU - Katrukha, Eugene A.

AU - Maidorn, Manuel

AU - Opazo, Felipe

AU - Moutel, Sandrine

AU - Vantard, Marilyn

AU - Perez, Frank

AU - van Bergen en Henegouwen, Paul M. P.

AU - Hoogenraad, Casper C.

AU - Ewers, Helge

AU - Kapitein, Lukas C.

PY - 2015/8/11

Y1 - 2015/8/11

N2 - Microtubules are hollow biopolymers of 25-nm diameter and are key constituents of the cytoskeleton. In neurons, microtubules are organized differently between axons and dendrites, but their precise organization in different compartments is not completely understood. Super-resolution microscopy techniques can detect specific structures at an increased resolution, but the narrow spacing between neuronal microtubules poses challenges because most existing labelling strategies increase the effective microtubule diameter by 20-40 nm and will thereby blend neighbouring microtubules into one structure. Here we develop single-chain antibody fragments (nanobodies) against tubulin to achieve super-resolution imaging of microtubules with a decreased apparent diameter. To test the resolving power of these novel probes, we generate microtubule bundles with a known spacing of 50-70 nm and successfully resolve individual microtubules. Individual bundled microtubules can also be resolved in different mammalian cells, including hippocampal neurons, allowing novel insights into fundamental mechanisms of microtubule organization in cell- and neurobiology.

AB - Microtubules are hollow biopolymers of 25-nm diameter and are key constituents of the cytoskeleton. In neurons, microtubules are organized differently between axons and dendrites, but their precise organization in different compartments is not completely understood. Super-resolution microscopy techniques can detect specific structures at an increased resolution, but the narrow spacing between neuronal microtubules poses challenges because most existing labelling strategies increase the effective microtubule diameter by 20-40 nm and will thereby blend neighbouring microtubules into one structure. Here we develop single-chain antibody fragments (nanobodies) against tubulin to achieve super-resolution imaging of microtubules with a decreased apparent diameter. To test the resolving power of these novel probes, we generate microtubule bundles with a known spacing of 50-70 nm and successfully resolve individual microtubules. Individual bundled microtubules can also be resolved in different mammalian cells, including hippocampal neurons, allowing novel insights into fundamental mechanisms of microtubule organization in cell- and neurobiology.

U2 - doi: 10.1038/ncomms8933

DO - doi: 10.1038/ncomms8933

M3 - SCORING: Journal article

VL - 6

JO - NAT COMMUN

JF - NAT COMMUN

SN - 2041-1723

IS - 7933

ER -