Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction

被引:69
作者
Satow, Reiko
Kurisaki, Akira
Chan, Te-chuan
Hamazaki, Tatsuo S.
Asashima, Makoto
机构
[1] Univ Tokyo, Grad Sch Sci, Dept Biol Sci, Bunkyo Ku, Tokyo 1138654, Japan
[2] Univ Tokyo, Grad Sch Arts & Sci, Dept Life Sci Biol, Meguro Ku, Tokyo 1538902, Japan
[3] Int Med Ctr Japan, Dept Tissue Regenerat, Inst Res, Shinjyuku Ku, Tokyo 1628655, Japan
[4] Japan Sci & Technol JST Agcy, Oran Regenerat Project, Meguro Ku, Tokyo 1538902, Japan
[5] Univ Tokushima, Inst Enzyme Res, Dept Mol Cytol, Tokushima 7708503, Japan
[6] Natl Inst Adv Ind Sci & Technol, Organ Dev Res Lab, Tsukuba, Ibaraki 3058562, Japan
基金
日本学术振兴会;
关键词
D O I
10.1016/j.devcel.2006.10.001
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Bone morphogenetic proteins (BMPs) regulate multiple biological processes, including cellular proliferation, adhesion, differentiation, and early development. In Xenopus development, inhibition of the BMP pathway is essential for neural induction. Here, we report that dullard, a gene involved in neural development, functions as a negative regulator of BMP signaling. We show that Dullard promotes the ubiquitin-mediated proteosomal degradation of BMP receptors (BMPRs). Dullard preferentially complexes with the BMP type 11 receptor (BMPRII) and partially colocalizes with the caveolin-1-positive compartment, suggesting that Dullard promotes BMPR degradation via the lipid raft-caveolar pathway. Dullard also associates with BMP type I receptors and represses the BMP-dependent phosphorylation of the BMP type I receptor. The phosphatase activity of Dullard is essential for the degradation of BMP receptors and neural induction in Xenopus. Together, these observations suggest that Dullard is an essential inhibitor of BMP receptor activation during Xenopus neuralization.
引用
收藏
页码:763 / 774
页数:12
相关论文
共 51 条
[1]   Two distinct pathways for inhibiting Pds1 ubiquitination in response to DNA damage [J].
Agarwal, R ;
Tang, ZY ;
Yu, HT ;
Cohen-Fix, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (45) :45027-45033
[2]   FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO [J].
Archambault, J ;
Pan, GH ;
Dahmus, GK ;
Cartier, M ;
Marshall, N ;
Zhang, S ;
Dahmus, ME ;
Greenblatt, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (42) :27593-27601
[3]   An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae [J].
Archambault, J ;
Chambers, RS ;
Kobor, MS ;
Ho, Y ;
Cartier, M ;
Bolotin, D ;
Andrews, B ;
Kane, CM ;
Greenblatt, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (26) :14300-14305
[4]   AP-2/Eps15 interaction is required for receptor-mediated endocytosis [J].
Benmerah, A ;
Lamaze, C ;
Bègue, B ;
Schmid, SL ;
Dautry-Varsat, A ;
Cerf-Bensussan, N .
JOURNAL OF CELL BIOLOGY, 1998, 140 (05) :1055-1062
[5]  
Candia AF, 1997, DEVELOPMENT, V124, P4467
[6]   A role for Xlim-1 in pronephros development in Xenopus laevis [J].
Chan, TC ;
Takahashi, S ;
Asashima, M .
DEVELOPMENTAL BIOLOGY, 2000, 228 (02) :256-269
[7]   Identification of phosphatases for Smad in the BMP/DPP pathway [J].
Chen, HB ;
Shen, JL ;
Ip, YT ;
Xu, L .
GENES & DEVELOPMENT, 2006, 20 (06) :648-653
[8]   A protein phosphatase functions to recycle RNA polymerase II [J].
Cho, H ;
Kim, TK ;
Mancebo, H ;
Lane, WS ;
Flores, O ;
Reinberg, D .
GENES & DEVELOPMENT, 1999, 13 (12) :1540-1552
[9]   c-Fos phosphorylation induced by H2O2 prevents proteasomal degradation of c-Fos in cardiomyocytes [J].
Coronella-Wood, J ;
Terrand, J ;
Sun, HP ;
Chen, QM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (32) :33567-33574
[10]   Smad-dependent and Smad-independent pathways in TGF-β family signalling [J].
Derynck, R ;
Zhang, YE .
NATURE, 2003, 425 (6958) :577-584