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Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor
Plant cell organelles are highly mobile and their positioning play key roles in plant growth, development and responses to changing environmental conditions. Movement is acto-myosin dependent. Despite controlling the dynamics of several organelles, myosin and myosin receptors identified so far in Ar...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8514473/ https://www.ncbi.nlm.nih.gov/pubmed/34645991 http://dx.doi.org/10.1038/s42003-021-02700-2 |
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author | Perico, Chiara Gao, Hongbo Heesom, Kate J. Botchway, Stanley W. Sparkes, Imogen A. |
author_facet | Perico, Chiara Gao, Hongbo Heesom, Kate J. Botchway, Stanley W. Sparkes, Imogen A. |
author_sort | Perico, Chiara |
collection | PubMed |
description | Plant cell organelles are highly mobile and their positioning play key roles in plant growth, development and responses to changing environmental conditions. Movement is acto-myosin dependent. Despite controlling the dynamics of several organelles, myosin and myosin receptors identified so far in Arabidopsis thaliana generally do not localise to the organelles whose movement they control, raising the issue of how specificity is determined. Here we show that a MyoB myosin receptor, MRF7, specifically localises to the Golgi membrane and affects its movement. Myosin XI-K was identified as a putative MRF7 interactor through mass spectrometry analysis. Co-expression of MRF7 and XI-K tail triggers the relocation of XI-K to the Golgi, linking a MyoB/myosin complex to a specific organelle in Arabidopsis. FRET-FLIM confirmed the in vivo interaction between MRF7 and XI-K tail on the Golgi and in the cytosol, suggesting that myosin/myosin receptor complexes perhaps cycle on and off organelle membranes. This work supports a traditional mechanism for organelle movement where myosins bind to receptors and adaptors on the organelle membranes, allowing them to actively move on the actin cytoskeleton, rather than passively in the recently proposed cytoplasmic streaming model. |
format | Online Article Text |
id | pubmed-8514473 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-85144732021-10-29 Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor Perico, Chiara Gao, Hongbo Heesom, Kate J. Botchway, Stanley W. Sparkes, Imogen A. Commun Biol Article Plant cell organelles are highly mobile and their positioning play key roles in plant growth, development and responses to changing environmental conditions. Movement is acto-myosin dependent. Despite controlling the dynamics of several organelles, myosin and myosin receptors identified so far in Arabidopsis thaliana generally do not localise to the organelles whose movement they control, raising the issue of how specificity is determined. Here we show that a MyoB myosin receptor, MRF7, specifically localises to the Golgi membrane and affects its movement. Myosin XI-K was identified as a putative MRF7 interactor through mass spectrometry analysis. Co-expression of MRF7 and XI-K tail triggers the relocation of XI-K to the Golgi, linking a MyoB/myosin complex to a specific organelle in Arabidopsis. FRET-FLIM confirmed the in vivo interaction between MRF7 and XI-K tail on the Golgi and in the cytosol, suggesting that myosin/myosin receptor complexes perhaps cycle on and off organelle membranes. This work supports a traditional mechanism for organelle movement where myosins bind to receptors and adaptors on the organelle membranes, allowing them to actively move on the actin cytoskeleton, rather than passively in the recently proposed cytoplasmic streaming model. Nature Publishing Group UK 2021-10-13 /pmc/articles/PMC8514473/ /pubmed/34645991 http://dx.doi.org/10.1038/s42003-021-02700-2 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Perico, Chiara Gao, Hongbo Heesom, Kate J. Botchway, Stanley W. Sparkes, Imogen A. Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title | Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title_full | Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title_fullStr | Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title_full_unstemmed | Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title_short | Arabidopsis thaliana myosin XIK is recruited to the Golgi through interaction with a MyoB receptor |
title_sort | arabidopsis thaliana myosin xik is recruited to the golgi through interaction with a myob receptor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8514473/ https://www.ncbi.nlm.nih.gov/pubmed/34645991 http://dx.doi.org/10.1038/s42003-021-02700-2 |
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