Glutamine-dependent Antiapoptotic Interaction of Human Glutaminyl-tRNA Synthetase with Apoptosis Signal-regulating Kinase 1

Ko, Young Gyu; Kim, Eun Kyoung; Kim, Sang Woo; Park, Heonyong; Park, Hee Sae; Choi, Eui Ju; Kim, Sung Hoon

doi:10.1074/jbc.m006189200

Cited by 181 publications

(137 citation statements)

References 51 publications

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“…ASK1 is negatively regulated by glutaminyl-tRNA synthetase, thioredoxin, glutathione S-transferase Mu, 14 -3-3, Akt, p21Cip1/WAF1, or HIV-1 Nef (7,(23)(24)(25)(26)(27)(28), implying that ASK1 is in a central position for apoptosis signaling. Here we added one more function of ASK1 in regard to the interaction with Daxx.…”

Section: Discussionmentioning

confidence: 99%

“…In addition to caspase activation cascade, Fas ligation initiates the activation of c-Jun N-terminal kinase/stress activated protein kinase (JNK/SAPK) (6,7). After Fas ligation, Fas recruits an adaptor protein called Daxx that interacts with apoptosis signal-regulating kinase 1 (ASK1) activating JNK/ SAPK and p38 MAPK by phosphorylation (8,9).…”

mentioning

confidence: 99%

“…ASK1 Kinase Assay and Reporter Gene Assay-The kinase activity of ASK1 was determined as described previously (7). For Gal4-tk-luciferase reporter gene assay, 293 cells grown in 24-well plates were cotransfected with the indicated plasmids, Gal4-tk-luciferase (50 ng), and tk-␤-galactosidase (50 ng).…”

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confidence: 99%

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Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm

Ko¹,

Kang²,

Park³

et al. 2001

Journal of Biological Chemistry

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103

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Although Daxx (death-associated protein) was first reported to mediate the apoptotic signal from Fas to JNK in the cytoplasm, other data suggested that Daxx is mainly located in the nucleus as a transcriptional regulator. Here, we demonstrated that cellular localization of Daxx could be determined by the relative concentration of a proapoptotic kinase, apoptosis signal-regulating kinase 1 (ASK1) by using immunofluorescence and transcriptional reporter assay. ASK1 sequestered Daxx in the cytoplasm and inhibited the repressive activity of Daxx in transcription. In addition, Daxx was bound to the activated Fas only in the presence of ASK1, accelerating the Fas-mediated apoptosis. These results suggest that Daxx requires ASK1 for its cytoplasmic localization and Fas-mediated signaling. Taken together, we could conclude that ASK1 controls the dual function of Daxx as a transcriptional repressor in the nucleus and as a proapoptotic signal mediator in the cytoplasm.Fas ligand is known to trigger apoptosis by binding to a specific receptor, Fas, which is a member of the tumor necrosis factor receptor family (1). Upon cellular activation by Fas ligand, the ligated Fas forms death-induced signal complex (DISC) 1 composed of Fas, Fas-associated death domain protein (FADD), and caspase-8 (2, 3). Recruitment of procaspase-8 to DISC leads to its proteolytic activation initiating a cascade of caspase activation that finally induces apoptosis. The activated Casp-8 stimulates proteolytic cleavage of Bcl-2 interacting protein (BID) that initiates cytochrome c release in the mitochondria (4). The release of cytochrome c triggers the formation of a complex containing Apaf1 and procaspase-9, which is then autocleaved to process the downstream effector procaspases such as caspase-3 (5). The processing of these caspases is followed by the cleavage of apoptotic substrates, leading to the disruption of important cellular processes, changes in cellular and nuclear morphology, and ultimately to cell death (2, 3).In addition to caspase activation cascade, Fas ligation initiates the activation of c-Jun N-terminal kinase/stress activated protein kinase (JNK/SAPK) (6, 7). After Fas ligation, Fas recruits an adaptor protein called Daxx that interacts with apoptosis signal-regulating kinase 1 (ASK1) activating JNK/ SAPK and p38 MAPK by phosphorylation (8, 9). The death domain of Fas interacts with Daxx, not competing with FADD (10). Since overexpression of Daxx sensitizes the Fas-mediated apoptosis, it is tempting to speculate that Daxx is an adaptor protein for Fas-mediated apoptosis (6). However, the role of Daxx as an adaptor linking ASK1 to Fas has been challenged because Daxx has not been localized in the cytoplasm but detected mainly in the nucleus, interacting with nuclear proteins such as centromeric protein (CENP-C), Pax3, and promyelocytic leukemia protein (PML) (11-15). The nuclear Daxx represses transcription possibly by recruiting histone deacetylase (11). It is finally thought that the Daxx-ASK1-JNK pathway would not be essential ...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm

Ko¹,

Kang²,

Park³

et al. 2001

Journal of Biological Chemistry

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103

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“…Recently, AARSs have been implicated in specific physiological responses, such as apoptosis (2), cellular growth (3), and angiogenesis (4). Tyrosyl-tRNA synthetase (TyrRS or YARS) is conserved in eukaryotes ranging from insects to humans, and multiple mutations have been identified in its catalytic domain.…”

Section: Dna Damage Repairmentioning

confidence: 99%

Acetylation promotes TyrRS nuclear translocation to prevent oxidative damage

Cao

Xiao

et al. 2017

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

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Tyrosyl-tRNA synthetase (TyrRS) is well known for its essential aminoacylation function in protein synthesis. Recently, TyrRS has been shown to translocate to the nucleus and protect against DNA damage due to oxidative stress. However, the mechanism of TyrRS nuclear localization has not yet been determined. Herein, we report that TyrRS becomes highly acetylated in response to oxidative stress, which promotes nuclear translocation. Moreover, p300/ CBP-associated factor (PCAF), an acetyltransferase, and sirtuin 1 (SIRT1), a NAD + -dependent deacetylase, regulate the nuclear localization of TyrRS in an acetylation-dependent manner. Oxidative stress increases the level of PCAF and decreases the level of SIRT1 and deacetylase activity, all of which promote the nuclear translocation of hyperacetylated TyrRS. Furthermore, TyrRS is primarily acetylated on the K244 residue near the nuclear localization signal (NLS), and acetylation inhibits the aminoacylation activity of TyrRS. Molecular dynamics simulations have shown that the in silico acetylation of K244 induces conformational changes in TyrRS near the NLS, which may promote the nuclear translocation of acetylated TyrRS. Herein, we show that the acetylated K244 residue of TyrRS protects against DNA damage in mammalian cells and zebrafish by activating DNA repair genes downstream of transcription factor E2F1. Our study reveals a previously unknown mechanism by which acetylation regulates an aminoacyl-tRNA synthetase, thus affecting the repair pathways for damaged DNA.

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“…Glutaminyl-tRNA synthetase inhibits the pro-apoptotic signaling pathway through glutamine-dependent interaction with apoptosis signal-regulating kinase 1 (35). KRS is a component of the human immunodeficiency virus type 1 (HIV-1) particle by interacting with its protein Gag (36,37) and suppresses pre-maturation of viral proteins by inhibiting HIV-1 protease (38).…”

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confidence: 99%

Do Aminoacyl-tRNA synthetases have biological functions other than in protein biosynthesis?

Park¹,

Kim²

2006

IUBMB Life (International Union of Biochemistry and Molecular B

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Glutamine-dependent Antiapoptotic Interaction of Human Glutaminyl-tRNA Synthetase with Apoptosis Signal-regulating Kinase 1

Cited by 181 publications

References 51 publications

Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm

Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm

Acetylation promotes TyrRS nuclear translocation to prevent oxidative damage

Do Aminoacyl-tRNA synthetases have biological functions other than in protein biosynthesis?

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