Two Subunits of the FoF1-ATPase Are Phosphorylated in the Inner Mitochondrial Membrane

Struglics, A.; Fredlund, Kenneth M.; Møller, Ian Max; Allen, John F.

doi:10.1006/bbrc.1998.8151

Cited by 30 publications

(29 citation statements)

References 23 publications

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“…1, (Sommarin et al, 1990); 2, (Struglics et al, 1998); 3, (Bykova et al, 2003a); 4, (Bykova et al, 2003b); 5, (Ito et al, 2009); 6, (Vidal et al, 1993); 7, (Lund et al, 2001); 8, (Takahashi et al, 2003); 9, (Sugiyama et al, 2008); 10, (Li et al, 2009); 11, (de la Fuente van Bentem et al, 2008); 12, (Nakagami et al, 2010); 13, (Meyer et al, 2012); 14, (Budde and Randall, 1990). …”

Section: Protein Phosphorylation In Plant Mitochondriamentioning

confidence: 99%

Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells

Havelund¹,

Thelen²,

Møller³

2013

Front. Plant Sci.

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Mitochondria fulfill some basic roles in all plant cells. They supply the cell with energy in the form of ATP and reducing equivalents [NAD(P)H] and they provide the cell with intermediates for a range of biosynthetic pathways. In addition to this, mitochondria contribute to a number of specialized functions depending on the tissue and cell type, as well as environmental conditions. We will here review the biochemistry and proteomics of mitochondria from non-green cells and organs, which differ from those of photosynthetic organs in a number of respects. We will briefly cover purification of mitochondria and general biochemical properties such as oxidative phosphorylation. We will then mention a few adaptive properties in response to water stress, seed maturation and germination, and the ability to function under hypoxic conditions. The discussion will mainly focus on Arabidopsis cell cultures, etiolated germinating rice seedlings and potato tubers as model plants. It will cover the general proteome as well as the posttranslational modification protein phosphorylation. To date 64 phosphorylated mitochondrial proteins with a total of 103 phosphorylation sites have been identified.

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Section: Protein Phosphorylation In Plant Mitochondriamentioning

confidence: 99%

Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells

Havelund¹,

Thelen²,

Møller³

2013

Front. Plant Sci.

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“…In vitro studies of tyrosine phosphorylation of mitochondria and protein solubilization Mitochondria (0.5-1 mg in 500 µl) were preincubated at 30°C for 3 min in the kinase buffer as described in Struglics et al [4] containing 10 mM MnCl 2 to stimulate tyrosine kinase activity [11], 20 µM oligomycin and 30 µg/ml rotenone as in Papa et al [6] to inhibit mitochondrial energy metabolism and when indicated, 100 µM H 2 O 2 or 2 mM orthovanadate. Then, 200 µM ATP was added (except in the control samples) and incubation was 1480 O. Augereau et al…”

Section: Preparation Of Brain Mitochondria and Submitochondrial Fractmentioning

confidence: 99%

“…However, the regulation of oxidative phosphorylation (OXPHOS) is still unclear, and the role played by ROS and protein phosphorylation remains elusive. For example, reversible protein phosphorylation has been investigated in the mitochondria [3][4][5][6][7], and results showed the existence of a cAMP-dependent protein kinase (PKA) in the inner mitochondrial membrane and matrix fraction. Of particular interest are data showing PKA-dependent phosphorylation of the 18-kDa (AQDQ) subunit of complex I [6] and of subunit I of cytochrome c oxidase * Corresponding author.…”

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confidence: 99%

Identification of tyrosine-phosphorylated proteins of the mitochondrial oxidative phosphorylation machinery

Augereau

Claverol

Boudes

et al. 2005

CMLS, Cell. Mol. Life Sci.

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The role of some serine/threonine kinases in the regulation of mitochondrial physiology is now well established, but little is known about mitochondrial tyrosine kinases. We showed that tyrosine phosphorylation of rat brain mitochondrial proteins was increased by in vitro addition of ATP and H2O2, and also during in situ ATP production at state 3, and maximal reactive oxygen species production. The Src kinase inhibitor PP2 decreased tyrosine phosphorylation and respiratory rates at state 3. We found that the 39-kDa subunit of complex I was tyrosine phosphorylated, and we identified putative tyrosine-phosphorylated subunits for the other complexes. We also have strong evidence that the FoF1-ATP synthase alpha chain is probably tyrosine-phosphorylated, but demonstrated that the beta chain is not. The tyrosine phosphatase PTP 1B was found in brain but not in muscle, heart or liver mitochondria. Our results suggest that tyrosine kinases and phosphatases are involved in the regulation of oxidative phosphorylation.

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“…Because phosphopeptides corresponding to AtpA and AtpF (encoding ␣ and B subunits of the F 0 F 1 -ATP synthase) were identified only in ⌬stp1, one possibility is that the decrease in hemolytic activity is, in part, due to by decreased function of F 0 F 1 -ATP synthase, leading to decreased CylA/CylB function. Evidence that protein phosphorylation inhibits the F 0 F 1 -ATP synthase is provided by recent studies that indicate that protein kinase C (PKC) phosphorylation of AtpB inhibits the activity of the mitochondrial F 0 F 1 -ATP synthase (85,86). Similarly, phosphorylation of AtpA by the serine/threonine protein kinase of Sulfolobus solfatarocus P2 is also suggested to decrease ATP synthase activity (87).…”

Section: Discussionmentioning

confidence: 99%

Serine/Threonine Phosphatase Stp1 Mediates Post-transcriptional Regulation of Hemolysin, Autolysis, and Virulence of Group B Streptococcus

Burnside

Lembo

Harrell

et al. 2011

Journal of Biological Chemistry

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Background:Signaling mediated by serine/threonine phosphatases during bacterial pathogenesis is not completely understood. Results: In Group B Streptococcus (GBS), Stp1 controls serine/threonine kinase function, post-transcriptional regulation of hemolysin, autolysis, and virulence. Conclusion: Although not essential for growth, Stp1 is critical for GBS pathogenesis. Significance: The importance of Stp1 in virulence and autolysis accentuates the possibility of using phosphatase inhibitors to decrease GBS infections.

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Two Subunits of the FoF1-ATPase Are Phosphorylated in the Inner Mitochondrial Membrane

Cited by 30 publications

References 23 publications

Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells

Biochemistry, proteomics, and phosphoproteomics of plant mitochondria from non-photosynthetic cells

Identification of tyrosine-phosphorylated proteins of the mitochondrial oxidative phosphorylation machinery

Serine/Threonine Phosphatase Stp1 Mediates Post-transcriptional Regulation of Hemolysin, Autolysis, and Virulence of Group B Streptococcus

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