Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins

Yanzhang Luo; Shengqi Xiang; Alessandra Lucini Paioni; Agnes Adler; Peter Jan Hooikaas; A S Jijumon; Carsten Janke; Anna Akhmanova; Marc Baldus

doi:10.1007/978-1-0716-1406-8_10

Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins

Yanzhang Luo, Shengqi Xiang, Alessandra Lucini Paioni, Agnes Adler, Peter Jan Hooikaas, A S Jijumon, Carsten Janke, Anna Akhmanova, Marc Baldus^*

^*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

Abstract

In this chapter, we describe the preparatory and spectroscopic procedures for conducting solid-state NMR experiments on microtubules (MTs) obtained from human cells and their complexes with microtubule-associated proteins (MAPs). Next to labeling and functional assembly of MTs and MT-MAP complexes, we discuss solid-state NMR approaches, including fast MAS and hyperpolarization methods that can be used to examine these systems. Such studies can provide novel insight into the dynamic properties of MTs and MT-MAP complexes.

Original language	English
Title of host publication	Structural Proteomics
Subtitle of host publication	High-Throughput Methods
Editors	Raymond J. Owens
Publisher	Humana Press
Pages	193-201
Number of pages	9
Edition	3
ISBN (Electronic)	978-1-0716-1406-8
ISBN (Print)	978-1-0716-1405-1, 978-1-0716-1408-2
DOIs	https://doi.org/10.1007/978-1-0716-1406-8_10
Publication status	Published - 2021

Publication series

Name	Methods in Molecular Biology
Volume	2305
ISSN (Print)	1064-3745
ISSN (Electronic)	1940-6029

Bibliographical note

Funding Information:
We thank Gert Folkers for helpful discussions and Johan van der Zwan for excellent technical support. This work was supported by the Dutch Science Foundation NWO (VENI grant 722.016.002 to SX, NWO-Groot grant 175.010.2009.002, and TOP-PUNT grant to MB) and by uNMR-NL, the National Roadmap Large-Scale NMR Facility of the Netherlands (grant 184.032.207). C.J. is supported by the grants ANR-10-IDEX-0001-02 PSL, ANR-11-LBX-0038, FRM DEQ20170336756. S.B. was supported by the FRM grant FDT201805005465, and CEFIPRA 5703-1, and J.A.S. by the European Union?s Horizon 2020 Marie Sk?o-dowska-Curie grant agreement No. 675737, and the FRM grant FDT201904008210.

Publisher Copyright:
© 2021, Springer Science+Business Media, LLC, part of Springer Nature.

Keywords

Microtubule-associated proteins
Microtubules
Protein dynamics
Protein interactions
Solid-state NMR spectroscopy

Access to Document

10.1007/978-1-0716-1406-8_10

978-1-0716-1406-8_10Final published version, 344 KBLicence: Taverne

Cite this

Luo, Y., Xiang, S., Paioni, A. L., Adler, A., Hooikaas, P. J., Jijumon, A. S., Janke, C., Akhmanova, A., & Baldus, M. (2021). Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins. In R. J. Owens (Ed.), Structural Proteomics: High-Throughput Methods (3 ed., pp. 193-201). (Methods in Molecular Biology; Vol. 2305). Humana Press. https://doi.org/10.1007/978-1-0716-1406-8_10

@inbook{c7c1862dec0c473fb4e193f0317ba9ce,

title = "Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins",

abstract = "In this chapter, we describe the preparatory and spectroscopic procedures for conducting solid-state NMR experiments on microtubules (MTs) obtained from human cells and their complexes with microtubule-associated proteins (MAPs). Next to labeling and functional assembly of MTs and MT-MAP complexes, we discuss solid-state NMR approaches, including fast MAS and hyperpolarization methods that can be used to examine these systems. Such studies can provide novel insight into the dynamic properties of MTs and MT-MAP complexes.",

keywords = "Microtubule-associated proteins, Microtubules, Protein dynamics, Protein interactions, Solid-state NMR spectroscopy",

author = "Yanzhang Luo and Shengqi Xiang and Paioni, {Alessandra Lucini} and Agnes Adler and Hooikaas, {Peter Jan} and Jijumon, {A S} and Carsten Janke and Anna Akhmanova and Marc Baldus",

note = "Funding Information: We thank Gert Folkers for helpful discussions and Johan van der Zwan for excellent technical support. This work was supported by the Dutch Science Foundation NWO (VENI grant 722.016.002 to SX, NWO-Groot grant 175.010.2009.002, and TOP-PUNT grant to MB) and by uNMR-NL, the National Roadmap Large-Scale NMR Facility of the Netherlands (grant 184.032.207). C.J. is supported by the grants ANR-10-IDEX-0001-02 PSL, ANR-11-LBX-0038, FRM DEQ20170336756. S.B. was supported by the FRM grant FDT201805005465, and CEFIPRA 5703-1, and J.A.S. by the European Union?s Horizon 2020 Marie Sk?o-dowska-Curie grant agreement No. 675737, and the FRM grant FDT201904008210. Publisher Copyright: {\textcopyright} 2021, Springer Science+Business Media, LLC, part of Springer Nature.",

year = "2021",

doi = "10.1007/978-1-0716-1406-8_10",

language = "English",

isbn = "978-1-0716-1405-1",

series = "Methods in Molecular Biology",

publisher = "Humana Press",

pages = "193--201",

editor = "Owens, {Raymond J. }",

booktitle = "Structural Proteomics",

edition = "3",

}

Luo, Y, Xiang, S, Paioni, AL, Adler, A, Hooikaas, PJ, Jijumon, AS, Janke, C, Akhmanova, A & Baldus, M 2021, Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins. in RJ Owens (ed.), Structural Proteomics: High-Throughput Methods. 3 edn, Methods in Molecular Biology, vol. 2305, Humana Press, pp. 193-201. https://doi.org/10.1007/978-1-0716-1406-8_10

Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins. / Luo, Yanzhang; Xiang, Shengqi; Paioni, Alessandra Lucini et al.
Structural Proteomics: High-Throughput Methods. ed. / Raymond J. Owens. 3. ed. Humana Press, 2021. p. 193-201 (Methods in Molecular Biology; Vol. 2305).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic › peer-review

TY - CHAP

T1 - Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins

AU - Luo, Yanzhang

AU - Xiang, Shengqi

AU - Paioni, Alessandra Lucini

AU - Adler, Agnes

AU - Hooikaas, Peter Jan

AU - Jijumon, A S

AU - Janke, Carsten

AU - Akhmanova, Anna

AU - Baldus, Marc

N1 - Funding Information: We thank Gert Folkers for helpful discussions and Johan van der Zwan for excellent technical support. This work was supported by the Dutch Science Foundation NWO (VENI grant 722.016.002 to SX, NWO-Groot grant 175.010.2009.002, and TOP-PUNT grant to MB) and by uNMR-NL, the National Roadmap Large-Scale NMR Facility of the Netherlands (grant 184.032.207). C.J. is supported by the grants ANR-10-IDEX-0001-02 PSL, ANR-11-LBX-0038, FRM DEQ20170336756. S.B. was supported by the FRM grant FDT201805005465, and CEFIPRA 5703-1, and J.A.S. by the European Union?s Horizon 2020 Marie Sk?o-dowska-Curie grant agreement No. 675737, and the FRM grant FDT201904008210. Publisher Copyright: © 2021, Springer Science+Business Media, LLC, part of Springer Nature.

PY - 2021

Y1 - 2021

N2 - In this chapter, we describe the preparatory and spectroscopic procedures for conducting solid-state NMR experiments on microtubules (MTs) obtained from human cells and their complexes with microtubule-associated proteins (MAPs). Next to labeling and functional assembly of MTs and MT-MAP complexes, we discuss solid-state NMR approaches, including fast MAS and hyperpolarization methods that can be used to examine these systems. Such studies can provide novel insight into the dynamic properties of MTs and MT-MAP complexes.

AB - In this chapter, we describe the preparatory and spectroscopic procedures for conducting solid-state NMR experiments on microtubules (MTs) obtained from human cells and their complexes with microtubule-associated proteins (MAPs). Next to labeling and functional assembly of MTs and MT-MAP complexes, we discuss solid-state NMR approaches, including fast MAS and hyperpolarization methods that can be used to examine these systems. Such studies can provide novel insight into the dynamic properties of MTs and MT-MAP complexes.

KW - Microtubule-associated proteins

KW - Microtubules

KW - Protein dynamics

KW - Protein interactions

KW - Solid-state NMR spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=85105440276&partnerID=8YFLogxK

U2 - 10.1007/978-1-0716-1406-8_10

DO - 10.1007/978-1-0716-1406-8_10

M3 - Chapter

C2 - 33950391

SN - 978-1-0716-1405-1

SN - 978-1-0716-1408-2

T3 - Methods in Molecular Biology

SP - 193

EP - 201

BT - Structural Proteomics

A2 - Owens, Raymond J.

PB - Humana Press

ER -

Solid-State NMR Spectroscopy for Studying Microtubules and Microtubule-Associated Proteins

Abstract

Publication series

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this