TY - JOUR
T1 - Role of apoptosis signal-regulating kinase 1 (ASK1) as an activator of the GAPDH-Siah1 stress-signaling cascade
AU - Tristan, Carlos A.
AU - Ramos, Adriana
AU - Shahani, Neelam
AU - Emiliani, Francesco E.
AU - Nakajima, Hidemitsu
AU - Noeh, Christopher C.
AU - Kato, Yoshinori
AU - Takeuchi, Tadayoshi
AU - Noguchi, Takuya
AU - Kadowaki, Hisae
AU - Sedlak, Thomas W.
AU - Ishizuka, Koko
AU - Ichijo, Hidenori
AU - Sawa, Akira
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2015/1/2
Y1 - 2015/1/2
N2 - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays roles in both energy maintenance, and stress signaling by forming a protein complex with seven in absentia homolog 1 (Siah1). Mechanisms to coordinate its glycolytic and stress cascades are likely to be very important for survival and homeostatic control of any living organism. Here we report that apoptosis signal-regulating kinase 1 (ASK1), a representative stress kinase, interacts with both GAPDH and Siah1 and is likely able to phosphorylate Siah1 at specific amino acid residues (Thr-70/Thr-74 and Thr-235/Thr-239). Phosphorylation of Siah1 by ASK1 triggers GAPDH-Siah1 stress signaling and activates a key downstream target, p300 acetyltransferase in the nucleus. This novel mechanism, together with the established S-nitrosylation/oxidation of GAPDH at Cys-150, provides evidence of how the stress signaling involving GAPDH is finely regulated. In addition, the present results imply crosstalk between the ASK1 and GAPDHSiah1 stress cascades.
AB - Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays roles in both energy maintenance, and stress signaling by forming a protein complex with seven in absentia homolog 1 (Siah1). Mechanisms to coordinate its glycolytic and stress cascades are likely to be very important for survival and homeostatic control of any living organism. Here we report that apoptosis signal-regulating kinase 1 (ASK1), a representative stress kinase, interacts with both GAPDH and Siah1 and is likely able to phosphorylate Siah1 at specific amino acid residues (Thr-70/Thr-74 and Thr-235/Thr-239). Phosphorylation of Siah1 by ASK1 triggers GAPDH-Siah1 stress signaling and activates a key downstream target, p300 acetyltransferase in the nucleus. This novel mechanism, together with the established S-nitrosylation/oxidation of GAPDH at Cys-150, provides evidence of how the stress signaling involving GAPDH is finely regulated. In addition, the present results imply crosstalk between the ASK1 and GAPDHSiah1 stress cascades.
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U2 - 10.1074/jbc.M114.596205
DO - 10.1074/jbc.M114.596205
M3 - Article
C2 - 25391652
AN - SCOPUS:84920535695
SN - 0021-9258
VL - 290
SP - 56
EP - 64
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 1
ER -