Search

Your search keyword '"Chazeau, Anaël"' showing total 24 results
Start Over Author "Chazeau, Anaël"
24 results on '"Chazeau, Anaël"'

5. TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

Author

van Beuningen, Sam F.B., Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y., Frias, Cátia P., Franker, Mariella A.M., Katrukha, Eugene A., Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T., Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A.F. Maarten, Post, Jan A., Akhmanova, Anna, Pasterkamp, R. Jeroen, Kapitein, Lukas C., de Graaff, Esther, and Hoogenraad, Casper C.

Published
2015
Full Text
View/download PDF

10. Dynein Regulator NDEL1 Controls Polarized Cargo Transport at the Axon Initial Segment

Author

Kuijpers, Marijn, van de Willige, Dieudonnée, Freal, Amélie, Chazeau, Anaël, Franker, Mariella A, Hofenk, Jasper, Rodrigues, Ricardo J Cordeiro, Kapitein, Lukas C, Akhmanova, Anna, Jaarsma, Dick, Hoogenraad, Casper C, Sub Cell Biology, Celbiologie, Neurosciences, Sub Cell Biology, and Celbiologie

Subjects
Ankyrins, 0301 basic medicine, Carrier Proteins/genetics, Ankyrins/metabolism, Neuroscience(all), Knockout, Dynein, Axons/metabolism, macromolecular substances, Biology, Ankyrin-G, Synaptic vesicle, axon initial segment, Motor protein, 03 medical and health sciences, Mice, NDEL1, Microtubule, Taverne, medicine, Animals, Axon, Cytoskeleton, Mice, Knockout, dynein, cargo trafficking, Synaptic Vesicles/metabolism, General Neuroscience, NudE, Dyneins, Axon initial segment, Axons, neuron, Transport protein, Cell biology, Protein Transport, 030104 developmental biology, medicine.anatomical_structure, Cytoskeleton/metabolism, Synaptic Vesicles, Neuron, Dyneins/metabolism, polarized transport, Carrier Proteins, NDE1
Abstract

The development and homeostasis of neurons relies heavily on the selective targeting of vesicles into axon and dendrites. Microtubule-based motor proteins play an important role in polarized transport; however, the sorting mechanism to exclude dendritic cargo from the axon is unclear. We show that the dynein regulator NDEL1 controls somatodendritic cargo transport at the axon initial segment (AIS). NDEL1 localizes to the AIS via an interaction with the scaffold protein Ankyrin-G. Depletion of NDEL1 or its binding partner LIS1 results in both cell-wide and local defects, including the non-polarized trafficking of dendritic cargo through the AIS. We propose a model in which LIS1 is a critical mediator of local NDEL1-based dynein activation at the AIS. By localizing to the AIS, NDEL1 facilitates the reversal of somatodendritic cargos in the proximal axon.

Published
2016
Full Text
View/download PDF

12. The HAUS Complex Is a Key Regulator of Non-centrosomal Microtubule Organization during Neuronal Development

Author

Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Celbiologie, Biomolecular Mass Spectrometry and Proteomics, Cunha-Ferreira, Inês, Chazeau, Anaël, Buijs, Robin R, Stucchi, Riccardo, Will, Lena, Pan, Xingxiu, Adolfs, Youri, van der Meer, Christiaan, Wolthuis, Joanna C, Kahn, Olga I, Schätzle, Philipp, Altelaar, Maarten, Pasterkamp, R Jeroen, Kapitein, Lukas C, Hoogenraad, Casper C, Sub Cell Biology, Afd Biomol.Mass Spect. and Proteomics, Celbiologie, Biomolecular Mass Spectrometry and Proteomics, Cunha-Ferreira, Inês, Chazeau, Anaël, Buijs, Robin R, Stucchi, Riccardo, Will, Lena, Pan, Xingxiu, Adolfs, Youri, van der Meer, Christiaan, Wolthuis, Joanna C, Kahn, Olga I, Schätzle, Philipp, Altelaar, Maarten, Pasterkamp, R Jeroen, Kapitein, Lukas C, and Hoogenraad, Casper C

Published
2018

13. The HAUS Complex Is a Key Regulator of Non-centrosomal Microtubule Organization during Neuronal Development

Author

TN groep Pasterkamp, Brain, CMM Sectie Celbiologie, CMM Groep Van Mil, Regenerative Medicine and Stem Cells, TN groep Joëls, Cunha-Ferreira, Inês, Chazeau, Anaël, Buijs, Robin R., Stucchi, Riccardo, Will, Lena, Pan, Xingxiu, Adolfs, Youri, van der Meer, Christiaan, Wolthuis, Joanna C., Kahn, Olga I., Schätzle, Philipp, Altelaar, Maarten, Pasterkamp, R. Jeroen, Kapitein, Lukas C., Hoogenraad, Casper C., TN groep Pasterkamp, Brain, CMM Sectie Celbiologie, CMM Groep Van Mil, Regenerative Medicine and Stem Cells, TN groep Joëls, Cunha-Ferreira, Inês, Chazeau, Anaël, Buijs, Robin R., Stucchi, Riccardo, Will, Lena, Pan, Xingxiu, Adolfs, Youri, van der Meer, Christiaan, Wolthuis, Joanna C., Kahn, Olga I., Schätzle, Philipp, Altelaar, Maarten, Pasterkamp, R. Jeroen, Kapitein, Lukas C., and Hoogenraad, Casper C.

Published
2018

14. Differentiation between Oppositely Oriented Microtubules Controls Polarized Neuronal Transport

Author

Tas, Roderick P, Chazeau, Anaël, Cloin, Bas M C, Lambers, Maaike L A, Hoogenraad, Casper C, Kapitein, Lukas C, Tas, Roderick P, Chazeau, Anaël, Cloin, Bas M C, Lambers, Maaike L A, Hoogenraad, Casper C, and Kapitein, Lukas C

Abstract

Microtubules are essential for polarized transport in neurons, but how their organization guides motor proteins to axons or dendrites is unclear. Because different motors recognize distinct microtubule properties, we used optical nanoscopy to examine the relationship between microtubule orientations, stability, and modifications. Nanometric tracking of motors to super-resolve microtubules and determine their polarity revealed that in dendrites, stable and acetylated microtubules are mostly oriented minus-end out, while dynamic and tyrosinated microtubules are oriented oppositely. In addition, microtubules with similar orientations and modifications form bundles that bias transport. Importantly, because the plus-end-directed Kinesin-1 selectively interacts with acetylated microtubules, this organization guides this motor out of dendrites and into axons. In contrast, Kinesin-3 prefers tyrosinated microtubules and can enter both axons and dendrites. This separation of distinct microtubule subsets into oppositely oriented bundles constitutes a key architectural principle of the neuronal microtubule cytoskeleton that enables polarized sorting by different motor proteins.

Published
2017

16. Studying neuronal microtubule organization and microtubule-associated proteins using single molecule localization microscopy

Author

Chazeau, Anaël, Katrukha, Eugene A, Hoogenraad, Casper C, Kapitein, Lukas C, Sub Cell Biology, and Celbiologie

Subjects
Hippocampal neurons, Taverne, dSTORM, Super-resolution microscopy, Fixation, Microtubules, Cytoskeleton
Abstract

The formation and maintenance of highly polarized neurons critically depends on the proper organization of the microtubule (MT) cytoskeleton. In axons, MTs are uniformly oriented with their plus-end pointing outward whereas in mature dendrites MTs have mixed orientations. MT organization and dynamics can be regulated by MT-associated proteins (MAPs). Plus-end tracking proteins are specialized MAPs that decorate plus-ends of growing MTs and regulate neuronal polarity, neurite extension, and dendritic spine morphology. Conventional fluorescence microscopy enables observation of specific cellular components through molecule-specific labeling but provides limited resolution (∼250 nm). Therefore, electron microscopy has until now provided most of our knowledge about the precise MT organization in neurons. In the past decade, super-resolution fluorescence microscopy techniques have emerged that circumvent the diffraction limit of light and enable high-resolution reconstruction of the MT network combined with selective protein labeling. However, preserving MT ultrastructure, MAP binding, high labeling density, and antibody specificity after fixation protocols is still quite challenging. In this chapter, we provide an optimized protocol for two-color direct stochastic optical reconstruction microscopy imaging of neuronal MTs together with their growing plus-ends to probe MT architecture and polarity.

Published
2016

18. Dynein Regulator NDEL1 Controls Polarized Cargo Transport at the Axon Initial Segment

Author

Sub Cell Biology, Celbiologie, Kuijpers, Marijn, van de Willige, Dieudonnée, Freal, Amélie, Chazeau, Anaël, Franker, Mariella A, Hofenk, Jasper, Rodrigues, Ricardo J Cordeiro, Kapitein, Lukas C, Akhmanova, Anna, Jaarsma, Dick, Hoogenraad, Casper C, Sub Cell Biology, Celbiologie, Kuijpers, Marijn, van de Willige, Dieudonnée, Freal, Amélie, Chazeau, Anaël, Franker, Mariella A, Hofenk, Jasper, Rodrigues, Ricardo J Cordeiro, Kapitein, Lukas C, Akhmanova, Anna, Jaarsma, Dick, and Hoogenraad, Casper C

Published
2016

20. TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

Author

van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, Hoogenraad, Casper C, van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, and Hoogenraad, Casper C

Abstract

Axon formation, the initial step in establishing neuronal polarity, critically depends on local microtubule reorganization and is characterized by the formation of parallel microtubule bundles. How uniform microtubule polarity is achieved during axonal development remains an outstanding question. Here, we show that the tripartite motif containing (TRIM) protein TRIM46 plays an instructive role in the initial polarization of neuronal cells. TRIM46 is specifically localized to the newly specified axon and, at later stages, partly overlaps with the axon initial segment (AIS). TRIM46 specifically forms closely spaced parallel microtubule bundles oriented with their plus-end out. Without TRIM46, all neurites have a dendrite-like mixed microtubule organization resulting in Tau missorting and altered cargo trafficking. By forming uniform microtubule bundles in the axon, TRIM46 is required for neuronal polarity and axon specification in vitro and in vivo. Thus, TRIM46 defines a unique axonal cytoskeletal compartment for regulating microtubule organization during neuronal development.

Published
2015

21. TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

Author

Dep Biologie, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, Sub Biomol.Mass Spect. and Proteomics, Celbiologie, van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, Hoogenraad, Casper C, Dep Biologie, Biomolecular Mass Spectrometry and Proteomics, Sub Cell Biology, Sub Biomol.Mass Spect. and Proteomics, Celbiologie, van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, and Hoogenraad, Casper C

Published
2015

22. TRIM46 Controls Neuronal Polarity and Axon Specification by Driving the Formation of Parallel Microtubule Arrays

Author

TN groep Pasterkamp, TN groep Joëls, Brain, van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, Hoogenraad, Casper C, TN groep Pasterkamp, TN groep Joëls, Brain, van Beuningen, Sam F B, Will, Lena, Harterink, Martin, Chazeau, Anaël, van Battum, Eljo Y, Frias, Cátia P, Franker, Mariella A M, Katrukha, Eugene A, Stucchi, Riccardo, Vocking, Karin, Antunes, Ana T, Slenders, Lotte, Doulkeridou, Sofia, Sillevis Smitt, Peter, Altelaar, A F Maarten, Post, Jan A, Akhmanova, Anna, Pasterkamp, R Jeroen, Kapitein, Lukas C, de Graaff, Esther, and Hoogenraad, Casper C

Published
2015

24. Studying neuronal microtubule organization and microtubule-associated proteins using single molecule localization microscopy.

Author

Chazeau A, Katrukha EA, Hoogenraad CC, and Kapitein LC

Subjects
Animals, Cell Culture Techniques, Cell Line, Tumor, Cells, Cultured, HeLa Cells, Hippocampus cytology, Humans, Lentivirus genetics, Microscopy, Fluorescence methods, Rats, Retinal Pigment Epithelium cytology, Retinal Pigment Epithelium metabolism, Staining and Labeling, Transfection, Axons metabolism, Cytoskeleton metabolism, Hippocampus metabolism, Microtubule-Associated Proteins metabolism, Microtubules metabolism
Abstract

The formation and maintenance of highly polarized neurons critically depends on the proper organization of the microtubule (MT) cytoskeleton. In axons, MTs are uniformly oriented with their plus-end pointing outward whereas in mature dendrites MTs have mixed orientations. MT organization and dynamics can be regulated by MT-associated proteins (MAPs). Plus-end tracking proteins are specialized MAPs that decorate plus-ends of growing MTs and regulate neuronal polarity, neurite extension, and dendritic spine morphology. Conventional fluorescence microscopy enables observation of specific cellular components through molecule-specific labeling but provides limited resolution (∼250 nm). Therefore, electron microscopy has until now provided most of our knowledge about the precise MT organization in neurons. In the past decade, super-resolution fluorescence microscopy techniques have emerged that circumvent the diffraction limit of light and enable high-resolution reconstruction of the MT network combined with selective protein labeling. However, preserving MT ultrastructure, MAP binding, high labeling density, and antibody specificity after fixation protocols is still quite challenging. In this chapter, we provide an optimized protocol for two-color direct stochastic optical reconstruction microscopy imaging of neuronal MTs together with their growing plus-ends to probe MT architecture and polarity., (Copyright © 2016 Elsevier Inc. All rights reserved.)

Published
2016
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results