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Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail
It has recently been found that among the 17 Arabidopsis myosins, six (XIC, XIE, XIK, XI-I, MYA1, and MYA2) have a major role in the motility of Golgi bodies and mitochondria in Nicotiana benthamiana and Nicotiana tabacum. Here, the same dominant negative tail fragments were also found to arrest the...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245463/ https://www.ncbi.nlm.nih.gov/pubmed/21914656 http://dx.doi.org/10.1093/jxb/err265 |
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author | Avisar, Dror Abu-Abied, Mohamad Belausov, Eduard Sadot, Einat |
author_facet | Avisar, Dror Abu-Abied, Mohamad Belausov, Eduard Sadot, Einat |
author_sort | Avisar, Dror |
collection | PubMed |
description | It has recently been found that among the 17 Arabidopsis myosins, six (XIC, XIE, XIK, XI-I, MYA1, and MYA2) have a major role in the motility of Golgi bodies and mitochondria in Nicotiana benthamiana and Nicotiana tabacum. Here, the same dominant negative tail fragments were also found to arrest the movement of Gogi bodies when transiently expressed in Arabidopsis plants. However, when a Golgi marker was transiently expressed in plants knocked out in these myosins, its movement was dramatically inhibited only in the xik mutant. In addition, a tail fragment of myosin XIK could inhibit the movement of several post-Golgi organelles, such as the trans-Golgi network, pre-vacuolar compartment, and endosomes, as well as total cytoplasmic streaming, suggesting that myosin XIK is a major player in cytoplasm kinetics. However, no co-localization of myosin tails with the arrested organelles was observed. Several deletion truncations of the myosin XIK tail were generated to corroborate function with localization. All deletion mutants possessing an inhibitory effect on organelle movement exhibited a diffuse cytoplasmic distribution. Point mutations in the tail of myosin XIK revealed that Arg1368 and Arg1443 are essential for its activity. These residues correspond to Lys1706 and Lys1779 from mouse myosin Va, which mediate the inhibitory head–tail interaction in this myosin. Therefore, such an interaction might underlie the dominant negative effect of truncated plant myosin tails and explain the mislocalization with target organelles. |
format | Online Article Text |
id | pubmed-3245463 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32454632011-12-23 Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail Avisar, Dror Abu-Abied, Mohamad Belausov, Eduard Sadot, Einat J Exp Bot Research Papers It has recently been found that among the 17 Arabidopsis myosins, six (XIC, XIE, XIK, XI-I, MYA1, and MYA2) have a major role in the motility of Golgi bodies and mitochondria in Nicotiana benthamiana and Nicotiana tabacum. Here, the same dominant negative tail fragments were also found to arrest the movement of Gogi bodies when transiently expressed in Arabidopsis plants. However, when a Golgi marker was transiently expressed in plants knocked out in these myosins, its movement was dramatically inhibited only in the xik mutant. In addition, a tail fragment of myosin XIK could inhibit the movement of several post-Golgi organelles, such as the trans-Golgi network, pre-vacuolar compartment, and endosomes, as well as total cytoplasmic streaming, suggesting that myosin XIK is a major player in cytoplasm kinetics. However, no co-localization of myosin tails with the arrested organelles was observed. Several deletion truncations of the myosin XIK tail were generated to corroborate function with localization. All deletion mutants possessing an inhibitory effect on organelle movement exhibited a diffuse cytoplasmic distribution. Point mutations in the tail of myosin XIK revealed that Arg1368 and Arg1443 are essential for its activity. These residues correspond to Lys1706 and Lys1779 from mouse myosin Va, which mediate the inhibitory head–tail interaction in this myosin. Therefore, such an interaction might underlie the dominant negative effect of truncated plant myosin tails and explain the mislocalization with target organelles. Oxford University Press 2012-01 2011-09-13 /pmc/articles/PMC3245463/ /pubmed/21914656 http://dx.doi.org/10.1093/jxb/err265 Text en © 2011 The Author(s). http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details) |
spellingShingle | Research Papers Avisar, Dror Abu-Abied, Mohamad Belausov, Eduard Sadot, Einat Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title | Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title_full | Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title_fullStr | Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title_full_unstemmed | Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title_short | Myosin XIK is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
title_sort | myosin xik is a major player in cytoplasm dynamics and is regulated by two amino acids in its tail |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245463/ https://www.ncbi.nlm.nih.gov/pubmed/21914656 http://dx.doi.org/10.1093/jxb/err265 |
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