CoA Synthase is in complex with p85αPI3K and affects PI3K signaling pathway

Breus, Oksana; Panasyuk, Ganna; Gout, Ivan; Filonenko, Valeriy; Nemazanyy, Ivan

doi:10.1016/j.bbrc.2009.05.102

Cited by 21 publications

(25 citation statements)

References 22 publications

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“…We have recently reported that CoAsy could form complexes with proteins which are part of signal transduction network [9,10]. Here we asked whether the formation of complex between EDC4 and CoAsy could be regulated in a growth factor dependent manner.…”

Section: Resultsmentioning

confidence: 98%

“…So far a number of CoAsy binding proteins including kinases and phosphatase (e.g., p85a subunit of PI3K, S6K1, Shp2PTP) were identified. These data allow us to speculate about involvement of signaling pathways in regulation of CoA biogenesis together with regulation of PanK activity [9][10][11]. However, to date the precise mechanisms of these regulations remain poorly understood.…”

Section: Discussionmentioning

confidence: 96%

“…The main components of MOM (phos-phatidylcholine and phosphatidylethanolamine) strongly activate both catalytic activities of CoAsy [8]. Exploring CoAsy interaction network we found and characterized a number of complexes including CoAsy and S6K1, p85a regulatory subunit of PI3K, Shp2PTP [9][10][11], implying that diverse signaling pathways may play a role in the regulation of CoA biosynthesis.…”

Section: Introductionmentioning

confidence: 87%

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EDC4 interacts with and regulates the dephospho‐CoA kinase activity of CoA synthase

et al. 2012

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a b s t r a c tCoenzyme A synthase (CoAsy) is a bifunctional enzyme which facilitates the last two steps of Coenzyme A biogenesis in higher eukaryotes. Here we describe that CoAsy forms a complex with enhancer of mRNA-decapping protein 4 (EDC4), a central scaffold component of processing bodies. CoAsy/ EDC4 complex formation is regulated by growth factors and is affected by cellular stresses. EDC4 strongly inhibits the dephospho-CoA kinase activity of CoAsy in vitro. Transient overexpression of EDC4 decreases cell proliferation, and further co-expression of CoAsy diminishes this effect. Here we report that EDC4 might contribute to regulation of CoA biosynthesis in addition to its scaffold function in processing bodies. Structured summary of protein interactions:CoAsy physically interacts with EDC4 by anti bait coimmunoprecipitation (View Interaction: 1, 2, 3)

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Section: Resultsmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 87%

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EDC4 interacts with and regulates the dephospho‐CoA kinase activity of CoA synthase

et al. 2012

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“…Knockdown of pantothenate kinase (pank) and coenzyme A synthase (COASY) using shRNAs also specifically decreased the viability of HER2/neu positive breast cancer cells (Baumann et al, unpublished results). Interestingly, COASY has been shown to interact with the PI3K pathway as well as with the mTOR/S6K pathway [19, 20]. The cytosolic pool of Acetyl-CoA that feeds the lipogenic phenotype is uniquely poised to serve as a rheostat for the metabolic state of the cell.…”

Section: Fatty Acid/lipid Synthesis and Regulationmentioning

confidence: 99%

Lipid biology of breast cancer

Baumann

Sevinsky

Conklin

2013

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Alterations in lipid metabolism have been reported in many types of cancer. Lipids have been implicated in the regulation of proliferation, differentiation, apoptosis, inflammation, autophagy, motility and membrane homeostasis. It is required that their biosynthesis is tightly regulated to ensure homeostasis and to prevent unnecessary energy expenditure. This review focuses on the emerging understanding of the role of lipids and lipogenic pathway regulation in breast cancer, including parallels drawn from the study of metabolic disease models, and suggestions on how these findings can potentially be exploited to promote gains in HER2/neu-positive breast cancer research.

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“…For p85 we have demonstrated an existence of functional complex of CoAsy on mitochondria. Unexpectedly, significant changes of PI3K signaling pathway activity were observed in experiments with siRNA-mediated CoAsy knockdown providing additional evidence of the role of CoA biosynthetic pathway in signal transduction [42,43].…”

mentioning

confidence: 88%

PI3K/mTOR/S6K signaling pathway – new players and new functional links

Filonenko

2013

Biopolym. Cell

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This review summarizes experimental data related to the studies of PI3K/mTOR/S6K signaling conducted at the department of cell signaling. Analysis of novel S6Ks protein-protein interactions provided valuable information for understanding molecular mechanisms of regulation of S6Ks functional activity and subcellular localization mediated by PKC, CK2 and ROC1 ubiquitin ligase. We discuss the identification and functional analysis of novel isoform of ribosomal protein S6 kinase -S6K2 and of mTOR kinase -mTORb, as well as their oncogenic properties. Identification of CoA synthase responsible for last two steps in CoA biosynthesis and characterization of its interactions with S6K1 and other signaling molecules uncovere a potential link between mTOR/S6K signaling pathway and energy metabolism through regulation of CoA biosynthesis. The data concerning new molecular mechanisms of CoA synthase regulation are presented.

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CoA Synthase is in complex with p85αPI3K and affects PI3K signaling pathway

Cited by 21 publications

References 22 publications

EDC4 interacts with and regulates the dephospho‐CoA kinase activity of CoA synthase

EDC4 interacts with and regulates the dephospho‐CoA kinase activity of CoA synthase

Lipid biology of breast cancer

PI3K/mTOR/S6K signaling pathway – new players and new functional links

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