Protein phosphorylation in isolated mitochondria and the effects of protein kinase C

Backer, Joseph M.; Arcoleo, J.P.; Weinstein, I. Bernard

doi:10.1016/0014-5793(86)80530-0

Cited by 13 publications

(5 citation statements)

References 15 publications

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“…These observations suggest a possible mitoStat3-PKC dependent mitochondrial import mechanism in response to TPA treatment. However, it is also possible that Stat3 is imported via a PKC independent mechanism and is phosphorylated by PKCε within mitochondria, as PKCs maintain kinase activity in mitochondria (Backer et al 1986). …”

Section: Discussionmentioning

confidence: 99%

Stat3 Binds to mtDNA and Regulates Mitochondrial Gene Expression in Keratinocytes

Macías

Rao

Carbajal

et al. 2014

Journal of Investigative Dermatology

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The nuclear transcription factor Stat3 has recently been reported to have a localized mitochondrial regulatory function. Current data suggest that mitochondrial Stat3 (mitoStat3) is necessary for maximal mitochondrial activity and for Ras-mediated transformation independent of Stat3 nuclear activity. We have previously shown that Stat3 plays a pivotal role in epithelial carcinogenesis. Therefore, the aim of the current study was to determine the role of mitoStat3 in epidermal keratinocytes. Herein, we show that normal and neoplastic keratinocytes contain a pool of mitoStat3. EGF and TPA induce Stat3 mitochondrial translocation mediated through phosphorylation of Stat3 at Ser727. In addition, we report that mitoStat3 binds mitochondrial DNA (mtDNA) and associates with the mitochondrial transcription factor TFAM. Furthermore, Stat3 ablation resulted in an increase of mitochondrial encoded gene transcripts. An increase in key nuclear-encoded metabolic genes, PGC-1α and NRF-1, was also observed in Stat3 null keratinocytes, however no changes in nuclear-encoded ETC gene transcripts or mtDNA copy number were observed. Collectively, our findings suggest a heretofore-unreported function for mitoStat3 as a potential mitochondrial transcription factor in keratinocytes. This mitoStat3-mtDNA interaction may represent an alternate signaling pathway that could alter mitochondrial function and biogenesis and play a role in tumorigenesis.

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Section: Discussionmentioning

confidence: 99%

Stat3 Binds to mtDNA and Regulates Mitochondrial Gene Expression in Keratinocytes

Macías

Rao

Carbajal

et al. 2014

Journal of Investigative Dermatology

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“…8). A 36 kDa phosphohistidine protein from rat mitochondria (Backer et al 1986) and a 37 kDa phosphohistidine protein from pea leaf mitochondria (Hakansson and Allen 1995) have also been reported. Since phosphohistidine proteins are often involved in signal transduction pathways, and have been predicted to be present in the inner mitochondrial membrane (Allen 1993a), the 37 kDa inner membrane bound phosphohistidine protein may be a sensor kinase of the bacterial type two-component signal transduction pathway (Parkinson and Kofoid 1992).…”

Section: The Individual Phosphoproteinsmentioning

confidence: 91%

Phosphoproteins and Protein Kinase Activities Intrinsic to Inner Membranes of Potato Tuber Mitochondria

Struglics

Fredlund

Allen

1999

Plant and Cell Physiology

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Inside-out submitochondrial particles (IO-SMP) were isolated and purified from potato (Solarium tuberosum L. cv.) tubers. When these IO-SMP were incubated with [y-32 P]ATP more then 20 proteins became labelled as a result of phosphorylation. The 32 P incorporation was stimulated by the oxidising reagent ferricyanide. Except for a 17 kDa protein which was phosphorylated only in the absence of divalent cations, the protein phosphorylation required Mg 2+ . The time for half-maximum 32 P incorporation was 4 min for the 22 kDa phospho-F, d'-subunit and 2 min for the 28 kDa phospho-F o b-subunit of the proton-ATPase. The K m for ATP for the detected phosphoproteins was between 65 fiM and 110 /

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“…149 Specific PKC isoforms can migrate to mitochondria upon activation, most likely by interacting with receptors for activated/inactive C-kinase (RACK/-RICK) 150,151 present on the outer membrane. PICK1 is one such PKC-interacting protein, and in NIH 3T3 cells, it was shown to be localized to mitochondria.…”

Section: Protein Kinase Cmentioning

confidence: 99%

Mitochondrial Protein Phosphorylation as a Regulatory Modality: Implications for Mitochondrial Dysfunction in Heart Failure

O’Rourke¹,

Eyk²,

Foster³

2011

Congestive Heart Failure

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Phosphorylation of mitochondrial proteins has been recognized for decades, and the regulation of pyruvate- and branched-chain α-ketoacid dehydrogenases by an atypical kinase/phosphatase cascade is well established. More recently, the development of new mass spectrometry-based technologies has led to the discovery of many novel phosphorylation sites on a variety of mitochondrial targets. The evidence suggests that the major classes of kinase and several phosphatases may be present at the mitochondrial outer membrane, intermembrane space, inner membrane, and matrix, but many questions remain to be answered as to the location, timing, and reversibility of these phosphorylation events and whether they are functionally relevant. The authors review phosphorylation as a mitochondrial regulatory strategy and highlight its possible role in the pathophysiology of cardiac hypertrophy and failure.

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Protein phosphorylation in isolated mitochondria and the effects of protein kinase C

Cited by 13 publications

References 15 publications

Stat3 Binds to mtDNA and Regulates Mitochondrial Gene Expression in Keratinocytes

Stat3 Binds to mtDNA and Regulates Mitochondrial Gene Expression in Keratinocytes

Phosphoproteins and Protein Kinase Activities Intrinsic to Inner Membranes of Potato Tuber Mitochondria

Mitochondrial Protein Phosphorylation as a Regulatory Modality: Implications for Mitochondrial Dysfunction in Heart Failure

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