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Pericentrin interacts with Kinesin-1 to drive centriole motility
Centrosome positioning is essential for their function. Typically, centrosomes are transported to various cellular locations through the interaction of centrosomal microtubules (MTs) with motor proteins anchored at the cortex or the nuclear surface. However, it remains unknown how centrioles migrate...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9361567/ https://www.ncbi.nlm.nih.gov/pubmed/35929834 http://dx.doi.org/10.1083/jcb.202112097 |
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author | Hannaford, Matthew R. Liu, Rong Billington, Neil Swider, Zachary T. Galletta, Brian J. Fagerstrom, Carey J. Combs, Christian Sellers, James R. Rusan, Nasser M. |
author_facet | Hannaford, Matthew R. Liu, Rong Billington, Neil Swider, Zachary T. Galletta, Brian J. Fagerstrom, Carey J. Combs, Christian Sellers, James R. Rusan, Nasser M. |
author_sort | Hannaford, Matthew R. |
collection | PubMed |
description | Centrosome positioning is essential for their function. Typically, centrosomes are transported to various cellular locations through the interaction of centrosomal microtubules (MTs) with motor proteins anchored at the cortex or the nuclear surface. However, it remains unknown how centrioles migrate in cellular contexts in which they do not nucleate MTs. Here, we demonstrate that during interphase, inactive centrioles move directly along the interphase MT network as Kinesin-1 cargo. We identify Pericentrin-Like-Protein (PLP) as a novel Kinesin-1 interacting molecule essential for centriole motility. In vitro assays show that PLP directly interacts with the cargo binding domain of Kinesin-1, allowing PLP to migrate on MTs. Binding assays using purified proteins revealed that relief of Kinesin-1 autoinhibition is critical for its interaction with PLP. Finally, our studies of neural stem cell asymmetric divisions in the Drosophila brain show that the PLP–Kinesin-1 interaction is essential for the timely separation of centrioles, the asymmetry of centrosome activity, and the age-dependent centrosome inheritance. |
format | Online Article Text |
id | pubmed-9361567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-93615672023-02-05 Pericentrin interacts with Kinesin-1 to drive centriole motility Hannaford, Matthew R. Liu, Rong Billington, Neil Swider, Zachary T. Galletta, Brian J. Fagerstrom, Carey J. Combs, Christian Sellers, James R. Rusan, Nasser M. J Cell Biol Article Centrosome positioning is essential for their function. Typically, centrosomes are transported to various cellular locations through the interaction of centrosomal microtubules (MTs) with motor proteins anchored at the cortex or the nuclear surface. However, it remains unknown how centrioles migrate in cellular contexts in which they do not nucleate MTs. Here, we demonstrate that during interphase, inactive centrioles move directly along the interphase MT network as Kinesin-1 cargo. We identify Pericentrin-Like-Protein (PLP) as a novel Kinesin-1 interacting molecule essential for centriole motility. In vitro assays show that PLP directly interacts with the cargo binding domain of Kinesin-1, allowing PLP to migrate on MTs. Binding assays using purified proteins revealed that relief of Kinesin-1 autoinhibition is critical for its interaction with PLP. Finally, our studies of neural stem cell asymmetric divisions in the Drosophila brain show that the PLP–Kinesin-1 interaction is essential for the timely separation of centrioles, the asymmetry of centrosome activity, and the age-dependent centrosome inheritance. Rockefeller University Press 2022-08-05 /pmc/articles/PMC9361567/ /pubmed/35929834 http://dx.doi.org/10.1083/jcb.202112097 Text en This is a work of the U.S. Government and is not subject to copyright protection in the United States. Foreign copyrights may apply. https://creativecommons.org/licenses/by-nc-sa/4.0/http://www.rupress.org/terms/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Hannaford, Matthew R. Liu, Rong Billington, Neil Swider, Zachary T. Galletta, Brian J. Fagerstrom, Carey J. Combs, Christian Sellers, James R. Rusan, Nasser M. Pericentrin interacts with Kinesin-1 to drive centriole motility |
title | Pericentrin interacts with Kinesin-1 to drive centriole motility |
title_full | Pericentrin interacts with Kinesin-1 to drive centriole motility |
title_fullStr | Pericentrin interacts with Kinesin-1 to drive centriole motility |
title_full_unstemmed | Pericentrin interacts with Kinesin-1 to drive centriole motility |
title_short | Pericentrin interacts with Kinesin-1 to drive centriole motility |
title_sort | pericentrin interacts with kinesin-1 to drive centriole motility |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9361567/ https://www.ncbi.nlm.nih.gov/pubmed/35929834 http://dx.doi.org/10.1083/jcb.202112097 |
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