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Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis
BACKGROUND: Protein palmitoylation, which is critical for membrane association and subcellular targeting of many signaling proteins, is catalyzed mainly by protein S-acyl transferases (PATs). Only a few plant proteins have been experimentally verified to be subject to palmitoylation, such as ROP GTP...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340681/ https://www.ncbi.nlm.nih.gov/pubmed/25849075 http://dx.doi.org/10.1186/s12870-015-0441-5 |
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author | Zhang, Yu-Ling Li, En Feng, Qiang-Nan Zhao, Xin-Ying Ge, Fu-Rong Zhang, Yan Li, Sha |
author_facet | Zhang, Yu-Ling Li, En Feng, Qiang-Nan Zhao, Xin-Ying Ge, Fu-Rong Zhang, Yan Li, Sha |
author_sort | Zhang, Yu-Ling |
collection | PubMed |
description | BACKGROUND: Protein palmitoylation, which is critical for membrane association and subcellular targeting of many signaling proteins, is catalyzed mainly by protein S-acyl transferases (PATs). Only a few plant proteins have been experimentally verified to be subject to palmitoylation, such as ROP GTPases, calcineurin B like proteins (CBLs), and subunits of heterotrimeric G proteins. However, emerging evidence from palmitoyl proteomics hinted that protein palmitoylation as a post-translational modification might be widespread. Nonetheless, due to the large number of genes encoding PATs and the lack of consensus motifs for palmitoylation, progress on the roles of protein palmitoylation in plants has been slow. RESULTS: We combined pharmacological and genetic approaches to examine the role of protein palmitoylation in root hair growth. Multiple PATs from different endomembrane compartments may participate in root hair growth, among which the Golgi-localized PAT24/TIP GROWTH DEFECTIVE1 (TIP1) plays a major role while the tonoplast-localized PAT10 plays a secondary role in root hair growth. A specific inhibitor for protein palmitoylation, 2-bromopalmitate (2-BP), compromised root hair elongation and polarity. Using various probes specific for cellular processes, we demonstrated that 2-BP impaired the dynamic polymerization of actin microfilaments (MF), the asymmetric plasma membrane (PM) localization of phosphatidylinositol (4,5)-bisphosphate (PIP(2)), the dynamic distribution of RabA4b-positive post-Golgi secretion, and endocytic trafficking in root hairs. CONCLUSIONS: By combining pharmacological and genetic approaches and using root hairs as a model, we show that protein palmitoylation, regulated by protein S-acyl transferases at different endomembrane compartments such as the Golgi and the vacuole, is critical for the polar growth of root hairs in Arabidopsis. Inhibition of protein palmitoylation by 2-BP disturbed key intracellular activities in root hairs. Although some of these effects are likely indirect, the cytological data reported here will contribute to a deep understanding of protein palmitoylation during tip growth in plants. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12870-015-0441-5) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4340681 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-43406812015-02-26 Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis Zhang, Yu-Ling Li, En Feng, Qiang-Nan Zhao, Xin-Ying Ge, Fu-Rong Zhang, Yan Li, Sha BMC Plant Biol Research Article BACKGROUND: Protein palmitoylation, which is critical for membrane association and subcellular targeting of many signaling proteins, is catalyzed mainly by protein S-acyl transferases (PATs). Only a few plant proteins have been experimentally verified to be subject to palmitoylation, such as ROP GTPases, calcineurin B like proteins (CBLs), and subunits of heterotrimeric G proteins. However, emerging evidence from palmitoyl proteomics hinted that protein palmitoylation as a post-translational modification might be widespread. Nonetheless, due to the large number of genes encoding PATs and the lack of consensus motifs for palmitoylation, progress on the roles of protein palmitoylation in plants has been slow. RESULTS: We combined pharmacological and genetic approaches to examine the role of protein palmitoylation in root hair growth. Multiple PATs from different endomembrane compartments may participate in root hair growth, among which the Golgi-localized PAT24/TIP GROWTH DEFECTIVE1 (TIP1) plays a major role while the tonoplast-localized PAT10 plays a secondary role in root hair growth. A specific inhibitor for protein palmitoylation, 2-bromopalmitate (2-BP), compromised root hair elongation and polarity. Using various probes specific for cellular processes, we demonstrated that 2-BP impaired the dynamic polymerization of actin microfilaments (MF), the asymmetric plasma membrane (PM) localization of phosphatidylinositol (4,5)-bisphosphate (PIP(2)), the dynamic distribution of RabA4b-positive post-Golgi secretion, and endocytic trafficking in root hairs. CONCLUSIONS: By combining pharmacological and genetic approaches and using root hairs as a model, we show that protein palmitoylation, regulated by protein S-acyl transferases at different endomembrane compartments such as the Golgi and the vacuole, is critical for the polar growth of root hairs in Arabidopsis. Inhibition of protein palmitoylation by 2-BP disturbed key intracellular activities in root hairs. Although some of these effects are likely indirect, the cytological data reported here will contribute to a deep understanding of protein palmitoylation during tip growth in plants. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12870-015-0441-5) contains supplementary material, which is available to authorized users. BioMed Central 2015-02-13 /pmc/articles/PMC4340681/ /pubmed/25849075 http://dx.doi.org/10.1186/s12870-015-0441-5 Text en © Zhang et al.; licensee BioMed Central. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Zhang, Yu-Ling Li, En Feng, Qiang-Nan Zhao, Xin-Ying Ge, Fu-Rong Zhang, Yan Li, Sha Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title | Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title_full | Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title_fullStr | Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title_full_unstemmed | Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title_short | Protein palmitoylation is critical for the polar growth of root hairs in Arabidopsis |
title_sort | protein palmitoylation is critical for the polar growth of root hairs in arabidopsis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340681/ https://www.ncbi.nlm.nih.gov/pubmed/25849075 http://dx.doi.org/10.1186/s12870-015-0441-5 |
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