Quantitation, network and function of protein phosphorylation in plant cell
Protein phosphorylation is one of the most important post-translational modifications (PTMs) as it participates in regulating various cellular processes and biological functions. It is therefore crucial to identify phosphorylated proteins to construct a phosphor-relay network, and eventually to unde...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2013-01-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00302/full |
| _version_ | 1818946394215415808 |
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| author | Lin eZHU Ning eLI |
| author_facet | Lin eZHU Ning eLI |
| author_sort | Lin eZHU |
| collection | DOAJ |
| description | Protein phosphorylation is one of the most important post-translational modifications (PTMs) as it participates in regulating various cellular processes and biological functions. It is therefore crucial to identify phosphorylated proteins to construct a phosphor-relay network, and eventually to understand the underlying molecular regulatory mechanism in response to both internal and external stimuli. The changes in phosphorylation status at these novel phosphosites can be accurately measured using a 15N-stable isotopic labeling in Arabidopsis (SILIA) quantitative proteomic approach in a high-throughput manner. One of the unique characteristics of the SILIA quantitative phosphoproteomic approach is the preservation of native PTM status on protein during the entire peptide preparation procedure. Evolved from SILIA is another quantitative PTM proteomic approach, AQUIP (absolute quantitation of isoforms of post-translationally modified proteins), which was developed by combining the advantages of targeted proteomics with SILIA. Bioinformatics-based phosphorylation site prediction coupled with an MS-based in vitro kinase assay is an additional way to extend the capability of phosphosite identification from the total cellular protein. The combined use of SILIA and AQUIP provides a novel strategy for molecular systems biological study and for investigation of in vivo biological functions of these phosphoprotein isoforms and combinatorial codes of PTMs. |
| first_indexed | 2024-12-20T08:14:19Z |
| format | Article |
| id | doaj.art-364378d7180f413183fdddb4b4c7ec11 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-20T08:14:19Z |
| publishDate | 2013-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-364378d7180f413183fdddb4b4c7ec112022-12-21T19:47:10ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2013-01-01310.3389/fpls.2012.0030237273Quantitation, network and function of protein phosphorylation in plant cellLin eZHU0Ning eLI1Hong Kong University of Science and TechnologyHong Kong University of Science and TechnologyProtein phosphorylation is one of the most important post-translational modifications (PTMs) as it participates in regulating various cellular processes and biological functions. It is therefore crucial to identify phosphorylated proteins to construct a phosphor-relay network, and eventually to understand the underlying molecular regulatory mechanism in response to both internal and external stimuli. The changes in phosphorylation status at these novel phosphosites can be accurately measured using a 15N-stable isotopic labeling in Arabidopsis (SILIA) quantitative proteomic approach in a high-throughput manner. One of the unique characteristics of the SILIA quantitative phosphoproteomic approach is the preservation of native PTM status on protein during the entire peptide preparation procedure. Evolved from SILIA is another quantitative PTM proteomic approach, AQUIP (absolute quantitation of isoforms of post-translationally modified proteins), which was developed by combining the advantages of targeted proteomics with SILIA. Bioinformatics-based phosphorylation site prediction coupled with an MS-based in vitro kinase assay is an additional way to extend the capability of phosphosite identification from the total cellular protein. The combined use of SILIA and AQUIP provides a novel strategy for molecular systems biological study and for investigation of in vivo biological functions of these phosphoprotein isoforms and combinatorial codes of PTMs.http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00302/fullPlantsCell signalingQuantitative ProteomicsPost translational Modifications (PTM)SILIAAQUIP |
| spellingShingle | Lin eZHU Ning eLI Quantitation, network and function of protein phosphorylation in plant cell Frontiers in Plant Science Plants Cell signaling Quantitative Proteomics Post translational Modifications (PTM) SILIA AQUIP |
| title | Quantitation, network and function of protein phosphorylation in plant cell |
| title_full | Quantitation, network and function of protein phosphorylation in plant cell |
| title_fullStr | Quantitation, network and function of protein phosphorylation in plant cell |
| title_full_unstemmed | Quantitation, network and function of protein phosphorylation in plant cell |
| title_short | Quantitation, network and function of protein phosphorylation in plant cell |
| title_sort | quantitation network and function of protein phosphorylation in plant cell |
| topic | Plants Cell signaling Quantitative Proteomics Post translational Modifications (PTM) SILIA AQUIP |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2012.00302/full |
| work_keys_str_mv | AT linezhu quantitationnetworkandfunctionofproteinphosphorylationinplantcell AT ningeli quantitationnetworkandfunctionofproteinphosphorylationinplantcell |