Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)

Agnes Adler; Lenette F Kjaer; J Wouter Beugelink; Marc Baldus; Hugo van Ingen

doi:10.1007/s12104-023-10124-8

Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)

Agnes Adler, Lenette F Kjaer, J Wouter Beugelink, Marc Baldus^*, Hugo van Ingen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The microtubule-associated protein 7 (MAP7) is a protein involved in cargo transport along microtubules (MTs) by interacting with kinesin-1 through the C-terminal kinesin-binding domain. Moreover, the protein is reported to stabilize MT, thereby playing a key role in axonal branch development. An important element for this latter function is the 112 amino-acid long N-terminal microtubule-binding domain (MTBD) of MAP7. Here we report NMR backbone and side-chain assignments that suggest a primarily alpha-helical secondary fold of this MTBD in solution. The MTBD contains a central long α-helical segment that includes a short four-residue 'hinge' sequence with decreased helicity and increased flexibility. Our data represent a first step towards analysing the complex interaction of MAP7 with MTs at an atomic level via NMR spectroscopy.

Original language	English
Pages (from-to)	83-88
Number of pages	6
Journal	Biomolecular NMR Assignments
Volume	17
Issue number	1
Early online date	26 Apr 2023
DOIs	https://doi.org/10.1007/s12104-023-10124-8
Publication status	Published - Jun 2023

Bibliographical note

Publisher Copyright:
© 2023, The Author(s).

Funding

This work was supported by NWO (the Dutch Science Foundation) via a TOP-PUNT (grant number 718.015.001) grant to MB and by uNMR-NL, the National Roadmap Large-Scale NMR Facility of the Netherlands (grant number 184.032.207).

Funders	Funder number
TOP-PUNT	184.032.207, 718.015.001
Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Keywords

MAP7
MTBD
Microtubule-associated proteins
Microtubules
NMR resonance assignments

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s12104-023-10124-8Final published version, 1.64 MBLicence: CC BY

Cite this

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abstract = "The microtubule-associated protein 7 (MAP7) is a protein involved in cargo transport along microtubules (MTs) by interacting with kinesin-1 through the C-terminal kinesin-binding domain. Moreover, the protein is reported to stabilize MT, thereby playing a key role in axonal branch development. An important element for this latter function is the 112 amino-acid long N-terminal microtubule-binding domain (MTBD) of MAP7. Here we report NMR backbone and side-chain assignments that suggest a primarily alpha-helical secondary fold of this MTBD in solution. The MTBD contains a central long α-helical segment that includes a short four-residue 'hinge' sequence with decreased helicity and increased flexibility. Our data represent a first step towards analysing the complex interaction of MAP7 with MTs at an atomic level via NMR spectroscopy.",

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AU - Beugelink, J Wouter

AU - Baldus, Marc

AU - van Ingen, Hugo

PY - 2023/6

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AB - The microtubule-associated protein 7 (MAP7) is a protein involved in cargo transport along microtubules (MTs) by interacting with kinesin-1 through the C-terminal kinesin-binding domain. Moreover, the protein is reported to stabilize MT, thereby playing a key role in axonal branch development. An important element for this latter function is the 112 amino-acid long N-terminal microtubule-binding domain (MTBD) of MAP7. Here we report NMR backbone and side-chain assignments that suggest a primarily alpha-helical secondary fold of this MTBD in solution. The MTBD contains a central long α-helical segment that includes a short four-residue 'hinge' sequence with decreased helicity and increased flexibility. Our data represent a first step towards analysing the complex interaction of MAP7 with MTs at an atomic level via NMR spectroscopy.

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Resonance assignments of the microtubule-binding domain of the microtubule-associated protein 7 (MAP7)

Abstract

Bibliographical note

Funding

Keywords

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