This enzyme is activated during Fas-mediated apoptosis. Following Fas ligation, the enzyme, which is constitutively phosphorylated, is dephosphorylated, and it is the dephosphorylated form that causes phosphorylation of TIA-1, a nuclear RNA-binding protein. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation.
This enzyme is activated during Fas-mediated apoptosis. Following Fas ligation, the enzyme, which is constitutively phosphorylated, is dephosphorylated, and it is the dephosphorylated form that causes phosphorylation of TIA-1, a nuclear RNA-binding protein. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation.
rapidly activated during Fas-mediated apoptosis. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation, suggesting a role in signaling downstream events in the apoptotic program
FAST serves as a sensor for mitochondrial stress modulating a TIA-1 regulated posttranscriptional stress response program, FAST might prevent TIA-1 mediated silencing of mRNA encoding inhibitors of of apoptosis
FAST K is known to interact with and phosphorylate TIA-1, effects of FAST K on other splicing factors and associated splicing regulatory motifs are mediated by changes in the function of TIA-1/TIAR, i.e. T-cell intracellular antigen 1 and TIA-related proteins, interaction analysis of FAST K with TIA, overview
FAST serves as a sensor for mitochondrial stress modulating a TIA-1 regulated posttranscriptional stress response program, FAST is a survival protein, modulating the NF-kappaB-dependent survival pathway, and has antiapoptotic effects inhibiting Fas-and UV-induced apoptosis, involving activation of caspase-3, its antiapoptotic effects are inhibited by TIA-1, FAST might prevent TIA-1 mediated silencing of mRNA encoding inhibitors of of apoptosis
Fas signaling is connected with the activity of splicing factors that modulate Fas alternative splicing, suggesting the existence of an autoregulatory loop that could serve to amplify Fas responses, overview
rapidly activated during Fas-mediated apoptosis. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation, suggesting a role in signaling downstream events in the apoptotic program
FAST serves as a sensor for mitochondrial stress modulating a TIA-1 regulated posttranscriptional stress response program, FAST might prevent TIA-1 mediated silencing of mRNA encoding inhibitors of of apoptosis
FAST K is known to interact with and phosphorylate TIA-1, effects of FAST K on other splicing factors and associated splicing regulatory motifs are mediated by changes in the function of TIA-1/TIAR, i.e. T-cell intracellular antigen 1 and TIA-related proteins, interaction analysis of FAST K with TIA, overview
FAST serves as a sensor for mitochondrial stress modulating a TIA-1 regulated posttranscriptional stress response program, FAST is a survival protein, modulating the NF-kappaB-dependent survival pathway, and has antiapoptotic effects inhibiting Fas-and UV-induced apoptosis, involving activation of caspase-3, its antiapoptotic effects are inhibited by TIA-1, FAST might prevent TIA-1 mediated silencing of mRNA encoding inhibitors of of apoptosis
Fas signaling is connected with the activity of splicing factors that modulate Fas alternative splicing, suggesting the existence of an autoregulatory loop that could serve to amplify Fas responses, overview
Thienopyrimidine-Chalcone Hybrid Molecules Inhibit Fas-Activated Serine/Threonine Kinase: An Approach To Ameliorate Antiproliferation in Human Breast Cancer Cells.
Accelerated FASTK mRNA degradation induced by oxidative stress is responsible for the destroyed myocardial mitochondrial gene expression and respiratory function in alcoholic cardiomyopathy.
Accelerated FASTK mRNA degradation induced by oxidative stress is responsible for the destroyed myocardial mitochondrial gene expression and respiratory function in alcoholic cardiomyopathy.
Thienopyrimidine-Chalcone Hybrid Molecules Inhibit Fas-Activated Serine/Threonine Kinase: An Approach To Ameliorate Antiproliferation in Human Breast Cancer Cells.
enzyme is phosphorylated on serine and threonine residues. In response to Fas ligation, it is rapidly dephosphorylated and concomitantly activated to phosphorylate TIA-1
the folding/unfolding transitions of urea-induced denaturation is monitored with the help of circular dichroism, intrinsic fluorescence, and UV absorption spectroscopies. Analysis of transition curves obtained from different probes reveal a coincidence of denaturation curves, suggesting that folding/unfolding of FASTK follows a two-state process with the midpoint (Cm) value at 3.50 M. Urea-induced denaturation curves are further analyzed to estimate change in the Gibbs free energy in the absence of urea (DGD0) associated with the equilibrium of denaturation. To get atomistic insights into the urea-induced denaturation of FASTK, an all-atom molecular dynamics simulation for 100 ns is performed
overexpression of HA-tagged enzyme in HeLa cells and in COS-7 cells, recombinant FAST promotes the expression of co-transfected reporter proteins, e.g. beta-galactosidase, via its TIA-1 binding domain, and increases the expression of endogenous cIAP-1 and XIAP, but not GAPDH, in HeLa cells
HA-tagged FAST K overexpression in HeLa cells enhances exon 6 inclusion of Fas reporters transfected in the cells, effects of FAST K are mediated by changes in the function of TIA-1/TIAR, i.e. T-cell intracellular antigen 1, and TIA-related proteins, the effects of FAST K overexpression are largely suppressed by depletion of TIA-1 and TIAR and are significantly compromised by mutation of a TIA-1/TIAR-responsive enhancer present downstream of exon 6 5' splice site, expression of GST-tagged TIA in HeLa cells
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the folding/unfolding transitions of urea-induced denaturation is monitored with the help of circular dichroism, intrinsic fluorescence, and UV absorption spectroscopies
Chemical-informatics approach to COVID-19 drug discovery Monte Carlo based QSAR, virtual screening and molecular docking study of some in-house molecules as papain-like protease (PLpro) inhibitors
Khan, N.S.; Khan, P.; Ansari, M.F.; Srivastava, S.; Hasan, G.M.; Husain, M.; Hassan, M.I.
Thienopyrimidine-chalcone hybrid molecules inhibit Fas-activated serine/threonine kinase an approach to ameliorate antiproliferation in human breast cancer cells