Cargando…
Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division
Cell polarity is a prerequisite for asymmetric cell divisions (ACDs) that generate cell type diversity during development of multicellular organisms. In Arabidopsis, stomatal lineage ACDs are regulated by the plant-specific protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE (BASL). BASL exhibits...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5014157/ https://www.ncbi.nlm.nih.gov/pubmed/27422992 http://dx.doi.org/10.1093/jxb/erw274 |
_version_ | 1782452254227300352 |
---|---|
author | Zhang, Ying Bergmann, Dominique C. Dong, Juan |
author_facet | Zhang, Ying Bergmann, Dominique C. Dong, Juan |
author_sort | Zhang, Ying |
collection | PubMed |
description | Cell polarity is a prerequisite for asymmetric cell divisions (ACDs) that generate cell type diversity during development of multicellular organisms. In Arabidopsis, stomatal lineage ACDs are regulated by the plant-specific protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE (BASL). BASL exhibits dynamic subcellular localization, accumulating initially in the nucleus, but then additionally in a highly polarized crescent at the cell cortex before division. BASL polarization requires a phosphorylation-mediated activation process, but how this is achieved remains unknown. In this study, we performed a fine-scale dissection of BASL protein subdomains and elucidated a nuclear localization sequence for nuclear import and a critical FxFP motif for cortical polarity formation, respectively. Artificially tethering BASL subdomains to the plasma membrane suggests that novel protein partner/s might exist and bind to an internal region of BASL. In addition, we suspect the existence of a protein degradation mechanism associated with the amino terminal domain of BASL that accounts for restricting its predominant expression to the stomatal lineage cells of the epidermis. Taken together, our results revealed that BASL, through its distinct subdomains, integrates multiple regulatory inputs to provide a mechanism that promotes difference during stomatal lineage ACDs. |
format | Online Article Text |
id | pubmed-5014157 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-50141572016-09-09 Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division Zhang, Ying Bergmann, Dominique C. Dong, Juan J Exp Bot Research Paper Cell polarity is a prerequisite for asymmetric cell divisions (ACDs) that generate cell type diversity during development of multicellular organisms. In Arabidopsis, stomatal lineage ACDs are regulated by the plant-specific protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE (BASL). BASL exhibits dynamic subcellular localization, accumulating initially in the nucleus, but then additionally in a highly polarized crescent at the cell cortex before division. BASL polarization requires a phosphorylation-mediated activation process, but how this is achieved remains unknown. In this study, we performed a fine-scale dissection of BASL protein subdomains and elucidated a nuclear localization sequence for nuclear import and a critical FxFP motif for cortical polarity formation, respectively. Artificially tethering BASL subdomains to the plasma membrane suggests that novel protein partner/s might exist and bind to an internal region of BASL. In addition, we suspect the existence of a protein degradation mechanism associated with the amino terminal domain of BASL that accounts for restricting its predominant expression to the stomatal lineage cells of the epidermis. Taken together, our results revealed that BASL, through its distinct subdomains, integrates multiple regulatory inputs to provide a mechanism that promotes difference during stomatal lineage ACDs. Oxford University Press 2016-09 2016-07-15 /pmc/articles/PMC5014157/ /pubmed/27422992 http://dx.doi.org/10.1093/jxb/erw274 Text en © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Zhang, Ying Bergmann, Dominique C. Dong, Juan Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title | Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title_full | Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title_fullStr | Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title_full_unstemmed | Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title_short | Fine-scale dissection of the subdomains of polarity protein BASL in stomatal asymmetric cell division |
title_sort | fine-scale dissection of the subdomains of polarity protein basl in stomatal asymmetric cell division |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5014157/ https://www.ncbi.nlm.nih.gov/pubmed/27422992 http://dx.doi.org/10.1093/jxb/erw274 |
work_keys_str_mv | AT zhangying finescaledissectionofthesubdomainsofpolarityproteinbaslinstomatalasymmetriccelldivision AT bergmanndominiquec finescaledissectionofthesubdomainsofpolarityproteinbaslinstomatalasymmetriccelldivision AT dongjuan finescaledissectionofthesubdomainsofpolarityproteinbaslinstomatalasymmetriccelldivision |