Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies.
The directional movement and positioning of organelles and macromolecules is essential for regulating and maintaining cellular functions in eukaryotic cells. In plants, these processes are actin-based and driven by class XI myosins, which transport various cargos in a directed manner. As the analysi...
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oai:doaj.org-article:16375288069c4be083dad7b18e9037122021-12-02T20:05:29ZUnravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies.1932-620310.1371/journal.pone.0252327https://doaj.org/article/16375288069c4be083dad7b18e9037122021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0252327https://doaj.org/toc/1932-6203The directional movement and positioning of organelles and macromolecules is essential for regulating and maintaining cellular functions in eukaryotic cells. In plants, these processes are actin-based and driven by class XI myosins, which transport various cargos in a directed manner. As the analysis of myosin function is challenging due to high levels of redundancy, dominant negative acting truncated myosins have frequently been used to study intracellular transport processes. A comparison of the dominant negative effect of the coiled-coil domains and the GTD domains revealed a much stronger inhibition of P-body movement by the GTD domains. In addition, we show that the GTD domain does not inhibit P-body movement when driven by a hybrid myosin in which the GTD domain was replaced by DCP2. These data suggest that the dominant negative effect of myosin tails involves a competition of the GTD domains for cargo binding sites.Lisa StephanMarc JakobyArijit DasEva KoebkeMartin HülskampPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 5, p e0252327 (2021) |
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Medicine R Science Q Lisa Stephan Marc Jakoby Arijit Das Eva Koebke Martin Hülskamp Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
description |
The directional movement and positioning of organelles and macromolecules is essential for regulating and maintaining cellular functions in eukaryotic cells. In plants, these processes are actin-based and driven by class XI myosins, which transport various cargos in a directed manner. As the analysis of myosin function is challenging due to high levels of redundancy, dominant negative acting truncated myosins have frequently been used to study intracellular transport processes. A comparison of the dominant negative effect of the coiled-coil domains and the GTD domains revealed a much stronger inhibition of P-body movement by the GTD domains. In addition, we show that the GTD domain does not inhibit P-body movement when driven by a hybrid myosin in which the GTD domain was replaced by DCP2. These data suggest that the dominant negative effect of myosin tails involves a competition of the GTD domains for cargo binding sites. |
format |
article |
author |
Lisa Stephan Marc Jakoby Arijit Das Eva Koebke Martin Hülskamp |
author_facet |
Lisa Stephan Marc Jakoby Arijit Das Eva Koebke Martin Hülskamp |
author_sort |
Lisa Stephan |
title |
Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
title_short |
Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
title_full |
Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
title_fullStr |
Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
title_full_unstemmed |
Unravelling the molecular basis of the dominant negative effect of myosin XI tails on P-bodies. |
title_sort |
unravelling the molecular basis of the dominant negative effect of myosin xi tails on p-bodies. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2021 |
url |
https://doaj.org/article/16375288069c4be083dad7b18e903712 |
work_keys_str_mv |
AT lisastephan unravellingthemolecularbasisofthedominantnegativeeffectofmyosinxitailsonpbodies AT marcjakoby unravellingthemolecularbasisofthedominantnegativeeffectofmyosinxitailsonpbodies AT arijitdas unravellingthemolecularbasisofthedominantnegativeeffectofmyosinxitailsonpbodies AT evakoebke unravellingthemolecularbasisofthedominantnegativeeffectofmyosinxitailsonpbodies AT martinhulskamp unravellingthemolecularbasisofthedominantnegativeeffectofmyosinxitailsonpbodies |
_version_ |
1718375467715657728 |