Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex

Haiwei Zhang; Hui Zhang; Yanquan Zhang; Ser Sur Ng; Fangli Ren; Yingying Wang; Yaqi Duan; Lin Chen; Yonggong Zhai; Qinglong Guo; Zhijie Chang

doi:10.1016/j.cellsig.2010.06.016

Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex

Haiwei Zhang, Hui Zhang, Yanquan Zhang, Ser Sur Ng, Fangli Ren, Yingying Wang, Yaqi Duan, Lin Chen, Yonggong Zhai, Qinglong Guo, Zhijie Chang

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

14 Scopus citations

Abstract

The TCF4/β-catenin complex, the executor of canonical Wnt/β-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases β-catenin from degradation and stabilizes TCF4/β-catenin complex. Here, we report that DDIP (Dishevelled- DEP domain Interacting Protein, also named as Spats1, spermatogenesis associated, serine-rich 1), a novel protein that interacts with Dvl, regulates Wnt signaling. We provide evidence that DDIP suppresses Lef-1 luciferase reporter activity stimulated by Wnt1, Dvl2 or β-catenin, interacts with the TCF4/β-catenin complex, and disrupts the interaction of TCF4 and β-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.

Original language	English
Pages (from-to)	1753-1760
Number of pages	8
Journal	Cellular Signalling
Volume	22
Issue number	11
DOIs	https://doi.org/10.1016/j.cellsig.2010.06.016
State	Published - Nov 2010

Keywords

DDIP
Dishevelled
Proteasome
TCF4/β-catenin complex

ASJC Scopus subject areas

Cell Biology

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10.1016/j.cellsig.2010.06.016

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title = "Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex",

abstract = "The TCF4/β-catenin complex, the executor of canonical Wnt/β-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases β-catenin from degradation and stabilizes TCF4/β-catenin complex. Here, we report that DDIP (Dishevelled- DEP domain Interacting Protein, also named as Spats1, spermatogenesis associated, serine-rich 1), a novel protein that interacts with Dvl, regulates Wnt signaling. We provide evidence that DDIP suppresses Lef-1 luciferase reporter activity stimulated by Wnt1, Dvl2 or β-catenin, interacts with the TCF4/β-catenin complex, and disrupts the interaction of TCF4 and β-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.",

keywords = "DDIP, Dishevelled, Proteasome, TCF4/β-catenin complex",

author = "Haiwei Zhang and Hui Zhang and Yanquan Zhang and Ng, {Ser Sur} and Fangli Ren and Yingying Wang and Yaqi Duan and Lin Chen and Yonggong Zhai and Qinglong Guo and Zhijie Chang",

year = "2010",

month = nov,

doi = "10.1016/j.cellsig.2010.06.016",

language = "English",

volume = "22",

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T1 - Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex

AU - Zhang, Haiwei

AU - Zhang, Hui

AU - Zhang, Yanquan

AU - Ng, Ser Sur

AU - Ren, Fangli

AU - Wang, Yingying

AU - Duan, Yaqi

AU - Chen, Lin

AU - Zhai, Yonggong

AU - Guo, Qinglong

AU - Chang, Zhijie

PY - 2010/11

Y1 - 2010/11

N2 - The TCF4/β-catenin complex, the executor of canonical Wnt/β-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases β-catenin from degradation and stabilizes TCF4/β-catenin complex. Here, we report that DDIP (Dishevelled- DEP domain Interacting Protein, also named as Spats1, spermatogenesis associated, serine-rich 1), a novel protein that interacts with Dvl, regulates Wnt signaling. We provide evidence that DDIP suppresses Lef-1 luciferase reporter activity stimulated by Wnt1, Dvl2 or β-catenin, interacts with the TCF4/β-catenin complex, and disrupts the interaction of TCF4 and β-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.

AB - The TCF4/β-catenin complex, the executor of canonical Wnt/β-catenin signaling, is regulated by a variety of factors. Among these, Dishevelled (Dvl) is a critical regulator that releases β-catenin from degradation and stabilizes TCF4/β-catenin complex. Here, we report that DDIP (Dishevelled- DEP domain Interacting Protein, also named as Spats1, spermatogenesis associated, serine-rich 1), a novel protein that interacts with Dvl, regulates Wnt signaling. We provide evidence that DDIP suppresses Lef-1 luciferase reporter activity stimulated by Wnt1, Dvl2 or β-catenin, interacts with the TCF4/β-catenin complex, and disrupts the interaction of TCF4 and β-catenin by promoting TCF4 degradation through the proteasome pathway. Our results indicate that DDIP is a negative regulator of the canonical Wnt signaling.

KW - DDIP

KW - Dishevelled

KW - Proteasome

KW - TCF4/β-catenin complex

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DO - 10.1016/j.cellsig.2010.06.016

M3 - Article

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AN - SCOPUS:77955657629

SN - 0898-6568

VL - 22

SP - 1753

EP - 1760

JO - Cellular Signalling

JF - Cellular Signalling

IS - 11

ER -

Dishevelled-DEP domain interacting protein (DDIP) inhibits Wnt signaling by promoting TCF4 degradation and disrupting the TCF4/β-catenin complex

Abstract

Keywords

ASJC Scopus subject areas

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