Projects per year
Abstract
The cargo-binding capabilities of cytoskeletal motor proteins have expanded during evolution through both gene duplication and alternative splicing. For the light chains of the kinesin-1 family of microtubule motors, this has resulted in an array of carboxyterminal domain sequences of unknown molecular function. Here, combining phylogenetic analyses with biophysical, biochemical and cell biology approaches we identify a highly conserved membrane-induced curvature-sensitive amphipathic helix within this region of a newly defined subset of long kinesin light chain paralogues and splice isoforms. This helix mediates the direct binding of kinesin-1 to lipid membranes. Membrane binding requires specific anionic phospholipids and is important for kinesin-1 dependent lysosome positioning, a canonical activity that until now has been attributed exclusively the recognition of organelle-associated cargo adaptor proteins. This leads us to propose a new protein-lipid coincidence detection framework for kinesin-1 mediated organelle transport.
Original language | English |
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Article number | eabg6636 |
Number of pages | 15 |
Journal | Science Advances |
Volume | 7 |
Issue number | 31 |
DOIs | |
Publication status | Published - 28 Jul 2021 |
Bibliographical note
Publisher Copyright:Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).
Research Groups and Themes
- BCS and TECS CDTs
- Bristol BioDesign Institute
- BrisSynBio
Keywords
- synthetic biology
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Dive into the research topics of 'Molecular mechanism for kinesin-1 direct membrane recognition'. Together they form a unique fingerprint.Projects
- 1 Finished
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8083 BrisSynBio NMR Facility
Sedgley, K. R. (Principal Investigator)
1/02/20 → 31/03/22
Project: Research