Dynamics of reversible protein phosphorylation in thylakoids of flowering plants: The roles of STN7, STN8 and TAP38
Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led...
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| Published in | Biochimica et biophysica acta Vol. 1807; no. 8; pp. 887 - 896 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.08.2011
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0005-2728 0006-3002 1879-2650 |
| DOI | 10.1016/j.bbabio.2010.08.002 |
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| Abstract | Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led to the detection of novel low-abundance thylakoid phosphoproteins and localised their phosphorylation sites. Three of the enzymes involved in phosphorylation/dephosphorylation cycles in thylakoids, the protein kinases STN7 and STN8 and the phosphatase TAP38/PPH1, have been characterised in the model species
Arabidopsis thaliana. Differential protein phosphorylation is associated with changes in illumination and various other environmental parameters, and has been implicated in several acclimation responses, the molecular mechanisms of which are only partly understood. The phenomenon of State Transitions, which enables rapid adaptation to short-term changes in illumination, has recently been shown to depend on reversible phosphorylation of LHCII by STN7-TAP38/PPH1. STN7 is also necessary for long-term acclimation responses that counteract imbalances in energy distribution between PSII and PSI by changing the rates of accumulation of their reaction-centre and light-harvesting proteins. Another aspect of photosynthetic acclimation, the modulation of thylakoid ultrastructure, depends on phosphorylation of PSII core proteins, mainly executed by STN8. Here we review recent advances in the characterisation of STN7, STN8 and TAP38/PPH1, and discuss their physiological significance within the overall network of thylakoid protein phosphorylation. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts.
►Mass spectrometry and genetic approaches have advanced the field of thylakoid protein phosphorylation research. ►28 thylakoid proteins have been identified so far to be subject to phosphorylation. ►Two protein kinases (STN7 and STN8) and one phosphatase (TAP38/PPH1) involved in thylakoid protein phosphorylation have been identified. ►Reversible LHCII phosphorylation is the best understood instance of thylakoid protein phosphorylation. ►Only for very phosphoproteins the physiological significance of reversible phosphorylation has been elucidated. |
|---|---|
| AbstractList | Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led to the detection of novel low-abundance thylakoid phosphoproteins and localised their phosphorylation sites. Three of the enzymes involved in phosphorylation/dephosphorylation cycles in thylakoids, the protein kinases STN7 and STN8 and the phosphatase TAP38/PPH1, have been characterised in the model species Arabidopsis thaliana. Differential protein phosphorylation is associated with changes in illumination and various other environmental parameters, and has been implicated in several acclimation responses, the molecular mechanisms of which are only partly understood. The phenomenon of State Transitions, which enables rapid adaptation to short-term changes in illumination, has recently been shown to depend on reversible phosphorylation of LHCII by STN7-TAP38/PPH1. STN7 is also necessary for long-term acclimation responses that counteract imbalances in energy distribution between PSII and PSI by changing the rates of accumulation of their reaction-centre and light-harvesting proteins. Another aspect of photosynthetic acclimation, the modulation of thylakoid ultrastructure, depends on phosphorylation of PSII core proteins, mainly executed by STN8. Here we review recent advances in the characterisation of STN7, STN8 and TAP38/PPH1, and discuss their physiological significance within the overall network of thylakoid protein phosphorylation. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts. Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led to the detection of novel low-abundance thylakoid phosphoproteins and localised their phosphorylation sites. Three of the enzymes involved in phosphorylation/dephosphorylation cycles in thylakoids, the protein kinases STN7 and STN8 and the phosphatase TAP38/PPH1, have been characterised in the model species Arabidopsis thaliana. Differential protein phosphorylation is associated with changes in illumination and various other environmental parameters, and has been implicated in several acclimation responses, the molecular mechanisms of which are only partly understood. The phenomenon of State Transitions, which enables rapid adaptation to short-term changes in illumination, has recently been shown to depend on reversible phosphorylation of LHCII by STN7-TAP38/PPH1. STN7 is also necessary for long-term acclimation responses that counteract imbalances in energy distribution between PSII and PSI by changing the rates of accumulation of their reaction-centre and light-harvesting proteins. Another aspect of photosynthetic acclimation, the modulation of thylakoid ultrastructure, depends on phosphorylation of PSII core proteins, mainly executed by STN8. Here we review recent advances in the characterisation of STN7, STN8 and TAP38/PPH1, and discuss their physiological significance within the overall network of thylakoid protein phosphorylation. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts.Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led to the detection of novel low-abundance thylakoid phosphoproteins and localised their phosphorylation sites. Three of the enzymes involved in phosphorylation/dephosphorylation cycles in thylakoids, the protein kinases STN7 and STN8 and the phosphatase TAP38/PPH1, have been characterised in the model species Arabidopsis thaliana. Differential protein phosphorylation is associated with changes in illumination and various other environmental parameters, and has been implicated in several acclimation responses, the molecular mechanisms of which are only partly understood. The phenomenon of State Transitions, which enables rapid adaptation to short-term changes in illumination, has recently been shown to depend on reversible phosphorylation of LHCII by STN7-TAP38/PPH1. STN7 is also necessary for long-term acclimation responses that counteract imbalances in energy distribution between PSII and PSI by changing the rates of accumulation of their reaction-centre and light-harvesting proteins. Another aspect of photosynthetic acclimation, the modulation of thylakoid ultrastructure, depends on phosphorylation of PSII core proteins, mainly executed by STN8. Here we review recent advances in the characterisation of STN7, STN8 and TAP38/PPH1, and discuss their physiological significance within the overall network of thylakoid protein phosphorylation. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts. Phosphorylation is the most common post-translational modification found in thylakoid membrane proteins of flowering plants, targeting more than two dozen subunits of all multiprotein complexes, including some light-harvesting proteins. Recent progress in mass spectrometry-based technologies has led to the detection of novel low-abundance thylakoid phosphoproteins and localised their phosphorylation sites. Three of the enzymes involved in phosphorylation/dephosphorylation cycles in thylakoids, the protein kinases STN7 and STN8 and the phosphatase TAP38/PPH1, have been characterised in the model species Arabidopsis thaliana. Differential protein phosphorylation is associated with changes in illumination and various other environmental parameters, and has been implicated in several acclimation responses, the molecular mechanisms of which are only partly understood. The phenomenon of State Transitions, which enables rapid adaptation to short-term changes in illumination, has recently been shown to depend on reversible phosphorylation of LHCII by STN7-TAP38/PPH1. STN7 is also necessary for long-term acclimation responses that counteract imbalances in energy distribution between PSII and PSI by changing the rates of accumulation of their reaction-centre and light-harvesting proteins. Another aspect of photosynthetic acclimation, the modulation of thylakoid ultrastructure, depends on phosphorylation of PSII core proteins, mainly executed by STN8. Here we review recent advances in the characterisation of STN7, STN8 and TAP38/PPH1, and discuss their physiological significance within the overall network of thylakoid protein phosphorylation. This article is part of a Special Issue entitled: Regulation of Electron Transport in Chloroplasts. ►Mass spectrometry and genetic approaches have advanced the field of thylakoid protein phosphorylation research. ►28 thylakoid proteins have been identified so far to be subject to phosphorylation. ►Two protein kinases (STN7 and STN8) and one phosphatase (TAP38/PPH1) involved in thylakoid protein phosphorylation have been identified. ►Reversible LHCII phosphorylation is the best understood instance of thylakoid protein phosphorylation. ►Only for very phosphoproteins the physiological significance of reversible phosphorylation has been elucidated. |
| Author | Leister, Dario Wunder, Tobias Pesaresi, Paolo Pribil, Mathias |
| Author_xml | – sequence: 1 givenname: Paolo surname: Pesaresi fullname: Pesaresi, Paolo organization: Dipartimento di Scienze Biomolecolari e Biotecnologie, Università degli studi di Milano, I-20133 Milano, Italy – sequence: 2 givenname: Mathias surname: Pribil fullname: Pribil, Mathias organization: Lehrstuhl für Molekularbiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany – sequence: 3 givenname: Tobias surname: Wunder fullname: Wunder, Tobias organization: Lehrstuhl für Molekularbiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany – sequence: 4 givenname: Dario surname: Leister fullname: Leister, Dario email: leister@lrz.uni-muenchen.de organization: Lehrstuhl für Molekularbiologie der Pflanzen (Botanik), Department Biologie I, Ludwig-Maximilians-Universität München, D-82152 Planegg-Martinsried, Germany |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20728426$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Acclimation Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana dephosphorylation electron transfer energy environmental factors Light light harvesting complex Light-Harvesting Protein Complexes - genetics Light-Harvesting Protein Complexes - metabolism lighting membrane proteins Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism phosphoproteins Phosphorylation - physiology Phosphorylation - radiation effects Photosynthesis Photosystem I Protein Complex - genetics Photosystem I Protein Complex - metabolism photosystem II Photosystem II Protein Complex - genetics Photosystem II Protein Complex - metabolism post-translational modification protein kinases Protein Kinases - genetics Protein Kinases - metabolism protein phosphorylation Protein-Serine-Threonine Kinases Regulation State transitions thylakoids Thylakoids - enzymology Thylakoids - genetics ultrastructure |
| Title | Dynamics of reversible protein phosphorylation in thylakoids of flowering plants: The roles of STN7, STN8 and TAP38 |
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