SIRT1 interacts with and protects glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from nuclear translocation: Implications for cell survival after irradiation

Joo, Hyun Jin; Woo, Seon Rang; Shen, Yan; Yun, Mi Yong; Shin, Hyun Jin; Park, Eun Ran; Kim, Su Hyeon; Park, Jeong Eun; Ju, Yeun Jin; Hong, Sung Hee; Hwang, Sang‐Gu; Cho, Myung‐Haing; Kim, Joon; Lee, Kee Ho

doi:10.1016/j.bbrc.2012.07.006

Cited by 33 publications

(30 citation statements)

References 29 publications

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“…In Drosophila , a large-scale two-hybrid interaction study indicated an interaction between GAPDH and dSir2 [37], while in human cells the nitrosylated form of GAPDH was shown to bind to SIRT1, the closest human homologue to yeast Sir2, and lead to SIRT1 nitrosylation [38]. GAPDH translocation to the nucleus promotes apoptosis in mammalian cells; an independent study found that SIRT1 depletion led to nuclear translocation of GAPDH in the absence of apoptotic stress [39]. Sir2-GAPDH links have also been observed in yeast cells.…”

Section: Discussionmentioning

confidence: 99%

Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

et al. 2013

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Sir2 is an NAD+-dependent histone deacetylase required to mediate transcriptional silencing and suppress rDNA recombination in budding yeast. We previously identified Tdh3, a glyceraldehyde 3-phosphate dehydrogenase (GAPDH), as a high expression suppressor of the lethality caused by Sir2 overexpression in yeast cells. Here we show that Tdh3 interacts with Sir2, localizes to silent chromatin in a Sir2-dependent manner, and promotes normal silencing at the telomere and rDNA. Characterization of specific TDH3 alleles suggests that Tdh3's influence on silencing requires nuclear localization but does not correlate with its catalytic activity. Interestingly, a genetic assay suggests that Tdh3, an NAD+-binding protein, influences nuclear NAD+ levels; we speculate that Tdh3 links nuclear Sir2 with NAD+ from the cytoplasm.

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Section: Discussionmentioning

confidence: 99%

Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

et al. 2013

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“…Nuclear GAPDH is acetylated at lysine 160 by the acetyltransferase p300/CBP, which in turn stimulates the acetylation and catalytic activity of p300/CBP (26). In addition, it is also reported that Sirt1 restrains GAPDH entering nuclear via direct interaction with GAPDH in a deacetylase activity-independent manner (27). It is an open question whether K254 acetylation affects the nuclear translocation of GAPDH.…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde-3-phosphate Dehydrogenase Is Activated by Lysine 254 Acetylation in Response to Glucose Signal

Liu

et al. 2014

Journal of Biological Chemistry

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Background: Glyceraldehyde-3-phosphate dehydrogenase is a pivotal glycolytic enzyme and implicated in many human cancers. Results: GAPDH acetylation promotes its activity in response to glucose via the action of PCAF and HDAC5. Conclusion: GAPDH acetylation promotes cell proliferation and tumor growth. Significance: This study demonstrates a critical role of GAPDH acetylation in tumor growth and provides potential therapy target for cancer.

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“…Another mechanism that prevents nuclear import of GAPDH under apoptotic conditions induced by irradiation has been described by Hyun-Yoo Joo and colleagues in 293T and Hela cells (Joo et al, 2012). They propose that Sirtuin1 (Sirt1) expression, but not its enzymatic activity, retains GAPDH in the cytosol.…”

Section: Nuclear Functions Of Gapdhmentioning

confidence: 98%

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

Hildebrandt¹,

Knuesting²,

Berndt³

et al. 2015

Biological Chemistry

149

131

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Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH, E.C. 1.2.1.12) is present in all organisms and catalyzes the oxidation of triose phosphate during glycolysis. GAPDH is one of the most prominent cellular targets of oxidative modifications when reactive oxygen and nitrogen species are formed during metabolism and under stress conditions. GAPDH harbors a strictly conserved catalytic cysteine, which is susceptible to a variety of thiol modifications, including S-sulfenylation, S-glutathionylation, S-nitrosylation, and S-sulfhydration. Upon reversible oxidative thiol modification of GAPDH, glycolysis is inhibited leading to a diversion of metabolic flux through the pentose-phosphate cycle to increase NADPH production. Furthermore, oxidized GAPDH may adopt new functions in different cellular compartments including the nucleus, as well as in new microcompartments associated with the cytoskeleton, mitochondria and plasma membrane. This review focuses on the recently discovered mechanism underlying the eminent reactivity between GAPDH and hydrogen peroxide and the subsequent redox-dependent moonlighting functions discriminating between the induction either of adaptive responses and adjustment of metabolism or of cell death in yeast, plants, and mammals. In light of the summarized results, cytosolic GAPDH might function as a sensor for redox signals and an information hub to transduce these signals for appropriate responses.

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SIRT1 interacts with and protects glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from nuclear translocation: Implications for cell survival after irradiation

Cited by 33 publications

References 29 publications

Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

Glyceraldehyde-3-phosphate Dehydrogenase Is Activated by Lysine 254 Acetylation in Response to Glucose Signal

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

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