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Plant Kinesin-12: Localization Heterogeneity and Functional Implications
Kinesin-12 family members are characterized by an N-terminal motor domain and the extensive presence of coiled-coil domains. Animal orthologs display microtubule plus-end directed motility, bundling of parallel and antiparallel microtubules, plus-end stabilization, and they play a crucial role in sp...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6747500/ https://www.ncbi.nlm.nih.gov/pubmed/31466291 http://dx.doi.org/10.3390/ijms20174213 |
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author | Müller, Sabine Livanos, Pantelis |
author_facet | Müller, Sabine Livanos, Pantelis |
author_sort | Müller, Sabine |
collection | PubMed |
description | Kinesin-12 family members are characterized by an N-terminal motor domain and the extensive presence of coiled-coil domains. Animal orthologs display microtubule plus-end directed motility, bundling of parallel and antiparallel microtubules, plus-end stabilization, and they play a crucial role in spindle assembly. In plants, kinesin-12 members mediate a number of developmental processes including male gametophyte, embryo, seedling, and seed development. At the cellular level, they participate in critical events during cell division. Several kinesin-12 members localize to the phragmoplast midzone, interact with isoforms of the conserved microtubule cross-linker MICROTUBULE-ASSOCIATED PROTEIN 65 (MAP65) family, and are required for phragmoplast stability and expansion, as well as for proper cell plate development. Throughout cell division, a subset of kinesin-12 reside, in addition or exclusively, at the cortical division zone and mediate the accurate guidance of the phragmoplast. This review aims to summarize the current knowledge on kinesin-12 in plants and shed some light onto the heterogeneous localization and domain architecture, which potentially conceals functional diversification. |
format | Online Article Text |
id | pubmed-6747500 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-67475002019-09-27 Plant Kinesin-12: Localization Heterogeneity and Functional Implications Müller, Sabine Livanos, Pantelis Int J Mol Sci Review Kinesin-12 family members are characterized by an N-terminal motor domain and the extensive presence of coiled-coil domains. Animal orthologs display microtubule plus-end directed motility, bundling of parallel and antiparallel microtubules, plus-end stabilization, and they play a crucial role in spindle assembly. In plants, kinesin-12 members mediate a number of developmental processes including male gametophyte, embryo, seedling, and seed development. At the cellular level, they participate in critical events during cell division. Several kinesin-12 members localize to the phragmoplast midzone, interact with isoforms of the conserved microtubule cross-linker MICROTUBULE-ASSOCIATED PROTEIN 65 (MAP65) family, and are required for phragmoplast stability and expansion, as well as for proper cell plate development. Throughout cell division, a subset of kinesin-12 reside, in addition or exclusively, at the cortical division zone and mediate the accurate guidance of the phragmoplast. This review aims to summarize the current knowledge on kinesin-12 in plants and shed some light onto the heterogeneous localization and domain architecture, which potentially conceals functional diversification. MDPI 2019-08-28 /pmc/articles/PMC6747500/ /pubmed/31466291 http://dx.doi.org/10.3390/ijms20174213 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Müller, Sabine Livanos, Pantelis Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title | Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title_full | Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title_fullStr | Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title_full_unstemmed | Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title_short | Plant Kinesin-12: Localization Heterogeneity and Functional Implications |
title_sort | plant kinesin-12: localization heterogeneity and functional implications |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6747500/ https://www.ncbi.nlm.nih.gov/pubmed/31466291 http://dx.doi.org/10.3390/ijms20174213 |
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