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Molecular mechanism for kinesin-1 direct membrane recognition

Research output: Contribution to journalArticlepeer-review

Zuriñe Antón, Johannes F. Weijman, Christopher Williams, Edmund R.R. Moody, Judith Mantell, Yan Y. Yip, Jessica A. Cross, Tom A. Williams, Roberto A. Steiner, Matthew P. Crump, Derek N. Woolfson, Mark P. Dodding

Original languageEnglish
Article numbereabg6636
JournalScience Advances
Issue number31
PublishedJul 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). Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

King's Authors


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 carboxyl-terminal 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 subset of long kinesin light-chain paralogs and splice isoforms. This helix mediates the direct binding of kinesin-1 to lipid membranes. Membrane binding requires specific anionic phospholipids, and it contributes to 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 protein-lipid coincidence detection framework for kinesin-1–mediated organelle transport.

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