Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7-Reference-Cited by-同舟云学术

Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7

Published:2022-01-21 Issue:6578 Volume:375 Page:326-331
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Ferro Luke S.¹^ORCID,Fang Qianglin¹^ORCID,Eshun-Wilson Lisa¹^ORCID,Fernandes Jonathan²^ORCID,Jack Amanda³^ORCID,Farrell Daniel P.⁴^ORCID,Golcuk Mert⁵^ORCID,Huijben Teun⁶^ORCID,Costa Katelyn⁷,Gur Mert⁵^ORCID,DiMaio Frank⁴,Nogales Eva¹³⁸⁹^ORCID,Yildiz Ahmet¹³⁹¹⁰^ORCID

Affiliation:

1. Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA.

2. Department of Chemistry, University of California, Berkeley, CA, USA.

3. Biophysics Graduate Group, University of California, Berkeley, CA, USA.

4. Department of Biochemistry, University of Washington, Seattle, WA, USA.

5. Department of Mechanical Engineering, Istanbul Technical University, Istanbul, Turkey.

6. Department of Imaging Physics, Delft University of Technology, Delft, Netherlands.

7. Press West Illustrations, Boston, MA, USA.

8. Howard Hughes Medical Institute, University of California, Berkeley, CA, USA.

9. Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA.

10. Physics Department, University of California, Berkeley, CA, USA.

Abstract

Microtubule (MT)–associated protein 7 (MAP7) is a required cofactor for kinesin-1–driven transport of intracellular cargoes. Using cryo–electron microscopy and single–molecule imaging, we investigated how MAP7 binds MTs and facilitates kinesin-1 motility. The MT-binding domain (MTBD) of MAP7 bound MTs as an extended α helix between the protofilament ridge and the site of lateral contact. Unexpectedly, the MTBD partially overlapped with the binding site of kinesin-1 and inhibited its motility. However, by tethering kinesin-1 to the MT, the projection domain of MAP7 prevented dissociation of the motor and facilitated its binding to available neighboring sites. The inhibitory effect of the MTBD dominated as MTs became saturated with MAP7. Our results reveal biphasic regulation of kinesin-1 by MAP7 in the context of their competitive binding to MTs.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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