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

Young-Gyu Ko, Young S. Kang, Heonyong Park, Wongi Seol, Jinyoung Kim, Taeho Kim, Hee S. Park, Eui Ju Choi, Sunghoon Kim

Research output: Contribution to journalArticle

101 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)39103-39106
Number of pages4
JournalJournal of Biological Chemistry
Volume276
Issue number42
DOIs
Publication statusPublished - 2001 Oct 19

Fingerprint

MAP Kinase Kinase Kinase 5
Cytoplasm
Proteins
Transcription
Fluorescent Antibody Technique
Assays
Phosphotransferases
Apoptosis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm. / Ko, Young-Gyu; Kang, Young S.; Park, Heonyong; Seol, Wongi; Kim, Jinyoung; Kim, Taeho; Park, Hee S.; Choi, Eui Ju; Kim, Sunghoon.

In: Journal of Biological Chemistry, Vol. 276, No. 42, 19.10.2001, p. 39103-39106.

Research output: Contribution to journalArticle

Ko, Young-Gyu ; Kang, Young S. ; Park, Heonyong ; Seol, Wongi ; Kim, Jinyoung ; Kim, Taeho ; Park, Hee S. ; Choi, Eui Ju ; Kim, Sunghoon. / Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 42. pp. 39103-39106.
@article{47be1da7a7fd44699da355f12d3fad01,
title = "Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm",
abstract = "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.",
author = "Young-Gyu Ko and Kang, {Young S.} and Heonyong Park and Wongi Seol and Jinyoung Kim and Taeho Kim and Park, {Hee S.} and Choi, {Eui Ju} and Sunghoon Kim",
year = "2001",
month = "10",
day = "19",
doi = "10.1074/jbc.M105928200",
language = "English",
volume = "276",
pages = "39103--39106",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "42",

}

TY - JOUR

T1 - Apoptosis Signal-regulating Kinase 1 Controls the Proapoptotic Function of Death-associated Protein (Daxx) in the Cytoplasm

AU - Ko, Young-Gyu

AU - Kang, Young S.

AU - Park, Heonyong

AU - Seol, Wongi

AU - Kim, Jinyoung

AU - Kim, Taeho

AU - Park, Hee S.

AU - Choi, Eui Ju

AU - Kim, Sunghoon

PY - 2001/10/19

Y1 - 2001/10/19

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0035914344&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035914344&partnerID=8YFLogxK

U2 - 10.1074/jbc.M105928200

DO - 10.1074/jbc.M105928200

M3 - Article

C2 - 11495919

AN - SCOPUS:0035914344

VL - 276

SP - 39103

EP - 39106

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 42

ER -