Tumor Suppressor NM23-H1 Is a Granzyme A-Activated DNase during CTL-Mediated Apoptosis, and the Nucleosome Assembly Protein SET Is Its Inhibitor

Fan, Zusen; Beresford, Paul J.; Oh, David Y.; Zhang, Dong; Lieberman, Judy

doi:10.1016/s0092-8674(03)00150-8

Cited by 491 publications

(291 citation statements)

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“…In addition to cell cycle regulation, SET also participates in a diversity of other functions as regulation of PP2A activity, chromatin remodeling and transcription, histone acetylation and apoptosis (Li et al, 1996;Okuwaki and Nagata, 1998;Seo et al, 2001;Cervoni et al, 2002;Fan et al, 2003). Thus, the association of GAPDH with SET could also be a new mechanism involved in the regulation of these cellular functions that merits to be explored in the next future.…”

Section: Discussionmentioning

confidence: 99%

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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We report here that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts in vitro and in vivo with the protein SET. This interaction is performed through the acidic domain of SET located at the carboxy terminal region. On analysing the functional relevance of SET-GAPDH interaction, we observed that GAPDH reverses in a dose-dependent manner, the inhibition of cyclin Bcdk1 activity produced by SET. Similarly to SET, GAPDH associates with cyclin B, suggesting that the regulation of cyclin B-cdk1 activity might be mediated not only by the interaction of GAPDH with SET but also with cyclin B. To analyse the putative role of GAPDH on cell cycle progression, HCT116 cells were transfected with a GAPDH expression vector. Results indicate that overexpression of GAPDH does not affect the timing of DNA replication but induces an increase in the number of mitosis, an advancement of the peak of cyclin B-cdk1 activity and an acceleration of cell cycle progression. All these results suggest that GAPDH might be involved in cell cycle regulation by modulating cyclin B-cdk1 activity.

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Section: Discussionmentioning

confidence: 99%

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

et al. 2006

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“…SET/TAF-I␤/INHAT was first identified as a translocation breakpoint-encoded protein in acute undifferentiated leukemia (22). It is a multifunctional protein that has been shown to bind preferentially to histone H3 (23)(24)(25), exhibit histone chaperone activity (26), interact with various factors such as DNA-binding proteins (27,28) and proteases (29), and regulate transcription (27,28,30,31), replication (32), and apoptosis (33). In addition, SET/TAF-I␤/ INHAT inhibits the activity of histone acetyltransferases, which suggests that it regulates the nuclear activity that arises from the chemical modification of core histones (34).…”

mentioning

confidence: 99%

Relationship between the structure of SET/TAF-Iβ/INHAT and its histone chaperone activity

Muto

Senda²,

Akai³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

149

185

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“…A large body of research also indicates that NM23/NDKs can interact directly with other proteins to regulate or provide links between different cellular pathways (17, 18). Of note is the presence of NM23-H1/NDK-A/DNase in a DNA repair complex, where it interacts with the exonuclease TREX1 to degrade DNA during granzyme A-mediated cell death (11,19) as well as the interactions of NM23-H2/NDK-B with integrin (20) and with a membrane receptor protein (21). Whether the developmental and cancer-related functions of NM23/NDP kinases are driven by the chemical reactions they catalyze and/or by their protein/protein regulatory interactions remains to be elucidated.…”

mentioning

confidence: 99%

Molecular and Functional Interactions between Escherichia coli Nucleoside-diphosphate Kinase and the Uracil-DNA Glycosylase Ung

Goswami¹,

Yoon

Abramczyk

et al. 2006

Journal of Biological Chemistry

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Escherichia coli nucleoside-diphosphate kinase (Ndk) catalyzes nucleoside triphosphate synthesis and maintains intracellular triphosphate pools. Mutants of E. coli lacking Ndk exhibit normal growth rates but show a mutator phenotype that cannot be entirely attributed to the absence of Ndk catalytic activity or to an imbalance in cellular triphosphates. It has been suggested previously that Ndk, similar to its human counterparts, possesses nuclease and DNA repair activities, including the excision of uracil from DNA, an activity normally associated with the Ung and Mug uracil-DNA glycosylases (UDGs) in E. coli. Here we have demonstrated that recombinant Ndk purified from wild-type E. coli contains significant UDG activity that is not intrinsic, but rather, is a consequence of a direct physical and functional interaction between Ung and Ndk, although a residual amount of intrinsic UDG activity exists as well. Co-purification of Ung and Ndk through multicolumn low pressure and nickel-nitrilotriacetic acid affinity chromatography suggests that the interaction occurs in a cellular context, as was also suggested by co-immunoprecipitation of endogenous Ung and Ndk from cellular extracts. Glutathione S-transferase pulldown and far Western analyses demonstrate that the interaction also occurs at the level of purified protein, suggesting that it is specific and direct. Moreover, significant augmentation of Ung catalytic activity by Ndk was observed, suggesting that the interaction between the two enzymes is functionally relevant. These findings represent the first example of Ung interacting with another E. coli protein and also lend support to the recently discovered role of nucleoside-diphosphate kinases as regulatory components of multiprotein complexes. Escherichia coli nucleoside-diphosphate (NDP)3 kinase (NDK, EC 2.7.4.6) belongs to a large family of highly conserved oligomeric phosphate transfer enzymes consisting of 4 -6 identically folded subunits of 16 -20 kDa, each containing an active site. NDP kinases catalyze the reversible transfer of ␥-phosphates between nucleoside di-and triphosphates at very high efficiencies through an evolutionarily conserved active site histidine residue (1-3). E. coli NDP kinase is encoded by a single gene, ndk (4), whereas the genetically distinct forms of human NDP kinases are encoded by multiple genes termed NM23-H1 through H8 (5). The name NM (nonmetastatic)23 was initially accorded to the matriarch of the family, NM23-H1, on the basis of its reported action as a tissue-specific metastasis inhibitor (6). Moreover, there is evidence that NM23/NDK proteins promote tumor formation and play various roles in normal development and cellular proliferation (7,8).NM23/NDP kinases are also multifunctional in vitro. In addition to the phosphoryl transfer reactions, they can catalyze various types of DNA cleavage (9 -12) and activate transcription (13-15). The involvement of NM23 in DNA repair was initially proposed on the basis of a covalent, lysine-mediated mechanism by which NM23-H2/NDK-B ...

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Tumor Suppressor NM23-H1 Is a Granzyme A-Activated DNase during CTL-Mediated Apoptosis, and the Nucleosome Assembly Protein SET Is Its Inhibitor

Cited by 491 publications

References 50 publications

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Glyceraldehyde 3-phosphate dehydrogenase is a SET-binding protein and regulates cyclin B-cdk1 activity

Relationship between the structure of SET/TAF-Iβ/INHAT and its histone chaperone activity

Molecular and Functional Interactions between Escherichia coli Nucleoside-diphosphate Kinase and the Uracil-DNA Glycosylase Ung

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