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...

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Autores principales:	Božena Klodová, Jan Fíla
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	phosphoproteomics pollen tube male gametophyte root hair signal transduction kinase motif Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/62831b7904ed49e8b5e2fbf010797346
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id	oai:doaj.org-article:62831b7904ed49e8b5e2fbf010797346
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spelling	oai:doaj.org-article:62831b7904ed49e8b5e2fbf0107973462021-11-25T17:54:22ZA Decade of Pollen Phosphoproteomics10.3390/ijms2222122121422-00671661-6596https://doaj.org/article/62831b7904ed49e8b5e2fbf0107973462021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12212https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Angiosperm 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 (<i>Arabidopsis thaliana</i>, 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.Božena KlodováJan FílaMDPI AGarticlephosphoproteomicspollen tubemale gametophyteroot hairsignal transductionkinase motifBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12212, p 12212 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	phosphoproteomics pollen tube male gametophyte root hair signal transduction kinase motif Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	phosphoproteomics pollen tube male gametophyte root hair signal transduction kinase motif Biology (General) QH301-705.5 Chemistry QD1-999 Božena Klodová Jan Fíla A Decade of Pollen Phosphoproteomics
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 (<i>Arabidopsis thaliana</i>, 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	article
author	Božena Klodová Jan Fíla
author_facet	Božena Klodová Jan Fíla
author_sort	Božena Klodová
title	A Decade of Pollen Phosphoproteomics
title_short	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_sort	decade of pollen phosphoproteomics
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/62831b7904ed49e8b5e2fbf010797346
work_keys_str_mv	AT bozenaklodova adecadeofpollenphosphoproteomics AT janfila adecadeofpollenphosphoproteomics AT bozenaklodova decadeofpollenphosphoproteomics AT janfila decadeofpollenphosphoproteomics
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A Decade of Pollen Phosphoproteomics

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