Molecular mechanism for kinesin-1 direct membrane recognition
| العنوان: | Molecular mechanism for kinesin-1 direct membrane recognition |
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| المؤلفون: | Zuriñe Antón, Judith Mantell, Jessica A. Cross, Edmund R. R. Moody, Yan Y. Yip, Tom A. Williams, Christopher Williams, Roberto A. Steiner, Derek N. Woolfson, Johannes F. Weijman, Mark P. Dodding, Matthew P. Crump |
| المصدر: | Science Advances Antón, Z, Weijman, J F, Williams, C, Moody, E R R, Mantell, J, Yip, Y Y, Cross, J A, Williams, T A, Steiner, R A, Crump, M, Woolfson, D N & Dodding, M P 2021, ' Molecular mechanism for kinesin-1 direct membrane recognition ', Science Advances, vol. 7, no. 31, eabg6636 . https://doi.org/10.1126/sciadv.abg6636Test |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | TERMINAL DOMAIN, Biophysics, Kinesins, BrisSynBio, CYTOSKELETON, macromolecular substances, Microtubules, Motor protein, BCS and TECS CDTs, 03 medical and health sciences, 0302 clinical medicine, Microtubule, Lysosome, Organelle, medicine, KINESIN, Health and Medicine, CYTOSKELETON, KINESIN, LIGHT-CHAIN, HEAVY-CHAIN, TERMINAL DOMAIN, PROTEIN CARGO BINDING IDENTIFICATION, MEMBRANE, Cytoskeleton, PROTEIN CARGO BINDING IDENTIFICATION, Phylogeny, Research Articles, 030304 developmental biology, Adaptor Proteins, Signal Transducing, 0303 health sciences, Multidisciplinary, LIGHT-CHAIN, Chemistry, Bristol BioDesign Institute, Alternative splicing, Signal transducing adaptor protein, SciAdv r-articles, HEAVY-CHAIN, Lipids, Cell biology, medicine.anatomical_structure, Kinesin, synthetic biology, MEMBRANE, 030217 neurology & neurosurgery, Research Article |
| الوصف: | Kinesin-1 uses a membrane-induced curvature-sensitive amphipathic helix to bind directly to cargo membranes. 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. |
| وصف الملف: | application/pdf |
| تدمد: | 2375-2548 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::744990a21f011918c47b011d869bcf35Test https://pubmed.ncbi.nlm.nih.gov/34321209Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....744990a21f011918c47b011d869bcf35 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 23752548 |
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