Cargando…
A Decade of Pollen Phosphoproteomics
Angiosperm mature pollen represents a quiescent stage with a desiccated cytoplasm surrounded by a tough cell wall, which is resistant to the suboptimal environmental conditions and carries the genetic information in an intact stage to the female gametophyte. Post pollination, pollen grains are rehyd...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619407/ https://www.ncbi.nlm.nih.gov/pubmed/34830092 http://dx.doi.org/10.3390/ijms222212212 |
_version_ | 1784604984076140544 |
---|---|
author | Klodová, Božena Fíla, Jan |
author_facet | Klodová, Božena Fíla, Jan |
author_sort | Klodová, Božena |
collection | PubMed |
description | Angiosperm mature pollen represents a quiescent stage with a desiccated cytoplasm surrounded by a tough cell wall, which is resistant to the suboptimal environmental conditions and carries the genetic information in an intact stage to the female gametophyte. Post pollination, pollen grains are rehydrated, activated, and a rapid pollen tube growth starts, which is accompanied by a notable metabolic activity, synthesis of novel proteins, and a mutual communication with female reproductive tissues. Several angiosperm species (Arabidopsis thaliana, tobacco, maize, and kiwifruit) were subjected to phosphoproteomic studies of their male gametophyte developmental stages, mostly mature pollen grains. The aim of this review is to compare the available phosphoproteomic studies and to highlight the common phosphoproteins and regulatory trends in the studied species. Moreover, the pollen phosphoproteome was compared with root hair phosphoproteome to pinpoint the common proteins taking part in their tip growth, which share the same cellular mechanisms. |
format | Online Article Text |
id | pubmed-8619407 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86194072021-11-27 A Decade of Pollen Phosphoproteomics Klodová, Božena Fíla, Jan Int J Mol Sci Review Angiosperm mature pollen represents a quiescent stage with a desiccated cytoplasm surrounded by a tough cell wall, which is resistant to the suboptimal environmental conditions and carries the genetic information in an intact stage to the female gametophyte. Post pollination, pollen grains are rehydrated, activated, and a rapid pollen tube growth starts, which is accompanied by a notable metabolic activity, synthesis of novel proteins, and a mutual communication with female reproductive tissues. Several angiosperm species (Arabidopsis thaliana, tobacco, maize, and kiwifruit) were subjected to phosphoproteomic studies of their male gametophyte developmental stages, mostly mature pollen grains. The aim of this review is to compare the available phosphoproteomic studies and to highlight the common phosphoproteins and regulatory trends in the studied species. Moreover, the pollen phosphoproteome was compared with root hair phosphoproteome to pinpoint the common proteins taking part in their tip growth, which share the same cellular mechanisms. MDPI 2021-11-11 /pmc/articles/PMC8619407/ /pubmed/34830092 http://dx.doi.org/10.3390/ijms222212212 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Klodová, Božena Fíla, Jan A Decade of Pollen Phosphoproteomics |
title | A Decade of Pollen Phosphoproteomics |
title_full | A Decade of Pollen Phosphoproteomics |
title_fullStr | A Decade of Pollen Phosphoproteomics |
title_full_unstemmed | A Decade of Pollen Phosphoproteomics |
title_short | A Decade of Pollen Phosphoproteomics |
title_sort | decade of pollen phosphoproteomics |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8619407/ https://www.ncbi.nlm.nih.gov/pubmed/34830092 http://dx.doi.org/10.3390/ijms222212212 |
work_keys_str_mv | AT klodovabozena adecadeofpollenphosphoproteomics AT filajan adecadeofpollenphosphoproteomics AT klodovabozena decadeofpollenphosphoproteomics AT filajan decadeofpollenphosphoproteomics |