CoA Synthase is phosphorylated on tyrosines in mammalian cells, interacts with and is dephosphorylated by Shp2PTP

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

doi:10.1007/s11010-009-0255-6

Cited by 15 publications

(12 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We have demonstrated that Shp2 mediates CoAsy dephosphorylation that leads to an increase in CoAsy enzymatic phosphopantetheine adenylyltransferase activity. We, therefore, argue that CoAsy is a novel potential substrate of Shp2 phosphatase and phosphorylation of CoAsy at tyrosine residue(s) could represent unrecognized before mechanism of modulation of intracellular CoA level in response to hormonal and/or other extracellular stimuli [44]. According to our data, Syk and Btk tyrosine kinases can modulate CoAsy phosphorylation in vitro and Src kinase in vivo as well.…”

supporting

confidence: 50%

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

Filonenko

2013

Biopolym. Cell

View full text Add to dashboard Cite

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.

show abstract

supporting

confidence: 50%

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

Filonenko

2013

Biopolym. Cell

View full text Add to dashboard Cite

show abstract

“…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%

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

et al. 2012

Self Cite

View full text Add to dashboard Cite

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)

show abstract

“…The enzyme activity can also be modulated by the cell's energy status, as high levels of ATP can displace CoA or its thioesters and support Pank activity [4]. The activity of CoA synthase, which mediates the last two steps of CoA biosynthesis, is also regulated by phospholipids and signalling pathways induced by extracellular stimuli and stresses [[5], [6], [7], [8]]. Dysregulation of CoA biosynthesis and homeostasis has been linked to human pathologies such as cancer, diabetes, neurodegeneration and cardiac hypertrophy [1,3].…”

Section: Introductionmentioning

confidence: 99%

Coenzyme A and protein CoAlation levels are regulated in response to oxidative stress and during morphogenesis in Dictyostelium discoideum

Aloum

Brimson

Zhyvoloup

et al. 2019

Biochemical and Biophysical Research Communications

Self Cite

View full text Add to dashboard Cite

Dictyostelium discoideum (D. discoideum) is a simple eukaryote with a unique life cycle in which it differentiates from unicellular amoebae into a fruiting body upon starvation. Reactive oxygen species (ROS) have been associated with bacterial predation, as well as regulatory events during D. discoideum development and differentiation. Coenzyme A (CoA) is a key metabolic integrator in all living cells. A novel function of CoA in redox regulation, mediated by covalent attachment of CoA to cellular proteins in response to oxidative or metabolic stress, has been recently discovered and termed protein CoAlation. In this study, we report that the level of CoA and protein CoAlation in D. discoideum are developmentally regulated, and correlate with the temporal expression pattern of genes implicated in CoA biosynthesis during morphogenesis. Furthermore, treatment of growing D. discoideum cells with oxidising agents results in a dose-dependent increase of protein CoAlation. However, much higher concentrations were required when compared to mammalian cells and bacteria. Increased resistance of D. discoideum to oxidative stress induced by H2O2 has previously been attributed to high levels of catalase activity. In support of this notion, we found that H2O2-induced protein CoAlation is significantly increased in CatA-deficient D. discoideum cells. Collectively, this study provides insights into the role of CoA and protein CoAlation in the maintenance of redox homeostasis in amoeba and during D. discoideum morphogenesis.

show abstract

CoA Synthase is phosphorylated on tyrosines in mammalian cells, interacts with and is dephosphorylated by Shp2PTP

Cited by 15 publications

References 21 publications

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

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

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

Coenzyme A and protein CoAlation levels are regulated in response to oxidative stress and during morphogenesis in Dictyostelium discoideum

Contact Info

Product

Resources

About