Functional identification of the pro-apoptotic effector domain in human Sox4

Eun Hye Hur; Wonhee Hur; Ju Youn Choi; In Kyung Kim; Ho Youn Kim; Seung Kew Yoon; Hyangshuk Rhim

doi:10.1016/j.bbrc.2004.09.215

Functional identification of the pro-apoptotic effector domain in human Sox4

Eun Hye Hur
, Wonhee Hur
, Ju Youn Choi
, In Kyung Kim
, Ho Youn Kim
, Seung Kew Yoon
, Hyangshuk Rhim

Division of Gastroenterology

The Catholic University of Korea
Sangmyung University
University of Ulsan

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

Recent studies provide evidence that Sox4 is involved in regulating apoptosis as well as tumorigenesis of various human cancers; however, its role in the apoptotic machinery is not fully understood. Here we describe that the central domain containing glycine-rich region in Sox4, named CD, is a pivotal pro-apoptotic domain to induce apoptotic cell death. Deletion of the DNA-binding domain or trans-activation domain in Sox4 did not significantly affect pro-apoptotic activity, whereas transient transfection of the high mobility group box or the serine-rich region abrogated the apoptotic activity. Moreover, overexpression of the CD construct (aa 166-342) revealed the apoptotic activity comparable to that of wild-type Sox4, approximately 60% of cell death. Our data suggest that the apoptotic activity of Sox4 can be dissociated from its transcriptional trans-activation and is mediated through its CD.

Original language	English
Pages (from-to)	59-67
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	325
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2004.09.215
State	Published - 3 Dec 2004

Bibliographical note

Funding Information:
We thank H. Clevers for the pCDM7-Sox4 plasmid. This study was supported by the Korean Research Foundation (KRF-99-041-D000344), the 2002 Specialized Research Center grant from the Korean Science and Engineering Foundation to the Rheumatism Research Center at The Catholic University of Korea (R11-2002-098-04003-0), and Korea Institute of Science and Technology Evaluation and Planning and Ministry of Science and Technology, Korean government, through its National Nuclear Technology Program (2004).

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Apoptosis
DNA-binding domain
Glycine-rich region
High mobility group
Serine-rich region
Sox4
trans-Activation domain

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10.1016/j.bbrc.2004.09.215

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title = "Functional identification of the pro-apoptotic effector domain in human Sox4",

abstract = "Recent studies provide evidence that Sox4 is involved in regulating apoptosis as well as tumorigenesis of various human cancers; however, its role in the apoptotic machinery is not fully understood. Here we describe that the central domain containing glycine-rich region in Sox4, named CD, is a pivotal pro-apoptotic domain to induce apoptotic cell death. Deletion of the DNA-binding domain or trans-activation domain in Sox4 did not significantly affect pro-apoptotic activity, whereas transient transfection of the high mobility group box or the serine-rich region abrogated the apoptotic activity. Moreover, overexpression of the CD construct (aa 166-342) revealed the apoptotic activity comparable to that of wild-type Sox4, approximately 60\% of cell death. Our data suggest that the apoptotic activity of Sox4 can be dissociated from its transcriptional trans-activation and is mediated through its CD.",

keywords = "Apoptosis, DNA-binding domain, Glycine-rich region, High mobility group, Serine-rich region, Sox4, trans-Activation domain",

author = "Hur, \{Eun Hye\} and Wonhee Hur and Choi, \{Ju Youn\} and Kim, \{In Kyung\} and Kim, \{Ho Youn\} and Yoon, \{Seung Kew\} and Hyangshuk Rhim",

note = "Funding Information: We thank H. Clevers for the pCDM7-Sox4 plasmid. This study was supported by the Korean Research Foundation (KRF-99-041-D000344), the 2002 Specialized Research Center grant from the Korean Science and Engineering Foundation to the Rheumatism Research Center at The Catholic University of Korea (R11-2002-098-04003-0), and Korea Institute of Science and Technology Evaluation and Planning and Ministry of Science and Technology, Korean government, through its National Nuclear Technology Program (2004).",

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doi = "10.1016/j.bbrc.2004.09.215",

language = "English",

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AU - Hur, Eun Hye

AU - Hur, Wonhee

AU - Choi, Ju Youn

AU - Kim, In Kyung

AU - Kim, Ho Youn

AU - Yoon, Seung Kew

AU - Rhim, Hyangshuk

N1 - Funding Information: We thank H. Clevers for the pCDM7-Sox4 plasmid. This study was supported by the Korean Research Foundation (KRF-99-041-D000344), the 2002 Specialized Research Center grant from the Korean Science and Engineering Foundation to the Rheumatism Research Center at The Catholic University of Korea (R11-2002-098-04003-0), and Korea Institute of Science and Technology Evaluation and Planning and Ministry of Science and Technology, Korean government, through its National Nuclear Technology Program (2004).

PY - 2004/12/3

Y1 - 2004/12/3

N2 - Recent studies provide evidence that Sox4 is involved in regulating apoptosis as well as tumorigenesis of various human cancers; however, its role in the apoptotic machinery is not fully understood. Here we describe that the central domain containing glycine-rich region in Sox4, named CD, is a pivotal pro-apoptotic domain to induce apoptotic cell death. Deletion of the DNA-binding domain or trans-activation domain in Sox4 did not significantly affect pro-apoptotic activity, whereas transient transfection of the high mobility group box or the serine-rich region abrogated the apoptotic activity. Moreover, overexpression of the CD construct (aa 166-342) revealed the apoptotic activity comparable to that of wild-type Sox4, approximately 60% of cell death. Our data suggest that the apoptotic activity of Sox4 can be dissociated from its transcriptional trans-activation and is mediated through its CD.

AB - Recent studies provide evidence that Sox4 is involved in regulating apoptosis as well as tumorigenesis of various human cancers; however, its role in the apoptotic machinery is not fully understood. Here we describe that the central domain containing glycine-rich region in Sox4, named CD, is a pivotal pro-apoptotic domain to induce apoptotic cell death. Deletion of the DNA-binding domain or trans-activation domain in Sox4 did not significantly affect pro-apoptotic activity, whereas transient transfection of the high mobility group box or the serine-rich region abrogated the apoptotic activity. Moreover, overexpression of the CD construct (aa 166-342) revealed the apoptotic activity comparable to that of wild-type Sox4, approximately 60% of cell death. Our data suggest that the apoptotic activity of Sox4 can be dissociated from its transcriptional trans-activation and is mediated through its CD.

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KW - DNA-binding domain

KW - Glycine-rich region

KW - High mobility group

KW - Serine-rich region

KW - Sox4

KW - trans-Activation domain

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M3 - Article

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SN - 0006-291X

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JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Functional identification of the pro-apoptotic effector domain in human Sox4

Abstract

Bibliographical note

UN SDGs

Keywords

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