Interaction of Arabidopsis BRASSINOSTEROID-INSENSITIVE 1 receptor kinase with a homolog of mammalian TGF-β receptor interacting protein

被引:53
作者
Ehsan, H
Ray, WK
Phinney, B
Wang, XF
Huber, SC
Clouse, SD [1 ]
机构
[1] N Carolina State Univ, Dept Hort Sci, Raleigh, NC 27695 USA
[2] Michigan State Univ, Michigan Proteome Consortium, E Lansing, MI 48824 USA
[3] Univ Illinois, USDA ARS, Photosynth Res Unit, Urbana, IL 61801 USA
基金
美国国家科学基金会;
关键词
brassinosteroids; BRI1; BAK1; TRIP-1; receptor kinase; TGF-beta;
D O I
10.1111/j.1365-313X.2005.02448.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Brassinosteroids (BRs) regulate multiple aspects of plant growth and development and require an active BRASSINOSTEROID-INSENSITIVE 1 (BRI1) receptor serine/threonine kinase for hormone perception and signal transduction. In mammals, the transforming growth factor-beta (TGF-beta) family of polypeptides modulate numerous aspects of development and are perceived at the cell surface by a complex of type I and type II TGF-beta receptor serine/threonine kinases. TGF-beta receptor interacting protein (TRIP-1) is a cytoplasmic substrate of the TGF-beta type II receptor kinase and plays a role in TGF-beta signaling. TRIP-1 is a WD domain protein that also functions as an essential subunit of the eIF3 eukaryotic translation initiation factor in animals, yeast and plants. We previously cloned putative TRIP-1 homologs from bean and Arabidopsis and found that transgenic Arabidopsis plants expressing antisense TRIP-1 RNA exhibited a broad range of developmental defects including some morphological characteristics that resemble the phenotype of BR-deficient and insensitive mutants. We now show that the BRI1 kinase domain phosphorylates Arabidopsis TRIP-1 on three specific sites in vitro (Thr-14, Thr-89 and either Thr-197 or Ser-198). Co-immunoprecipitation experiments using antibodies against TRIP-1, BRI1 and various fusion proteins strongly suggest that TRIP-1 and BRI1 also interact directly in vivo. These findings support a role for TRIP-1 in the molecular mechanisms of BR-regulated plant growth and development, possibly as a cytoplasmic substrate of the BRI1 receptor kinase.
引用
收藏
页码:251 / 261
页数:11
相关论文
共 49 条
[1]   Molecular physiology of brassinosteroids revealed by the analysis of mutants [J].
Altmann, T .
PLANTA, 1999, 208 (01) :1-11
[2]   Conservation and diversity of eukaryotic translation initiation factor eIF3 [J].
Asano, K ;
Kinzy, TG ;
Merrick, WC ;
Hershey, JWB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (02) :1101-1109
[3]   Receptor kinase signaling in plant development [J].
Becraft, PW .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2002, 18 :163-192
[4]   Brassinosteroids and plant steroid hormone signaling [J].
Bishop, GJ ;
Koncz, C .
PLANT CELL, 2002, 14 :S97-S110
[5]   Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase [J].
Bower, MS ;
Matias, DD ;
FernandesCarvalho, E ;
Mazzurco, M ;
Gu, TS ;
Rothstein, SJ ;
Goring, DR .
PLANT CELL, 1996, 8 (09) :1641-1650
[6]   Plant initiation factor 3 subunit composition resembles mammalian initiation factor 3 and has a novel subunit [J].
Burks, EA ;
Bezerra, PP ;
Le, H ;
Gallie, DR ;
Browning, KS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (03) :2122-2131
[7]   A WD-DOMAIN PROTEIN THAT IS ASSOCIATED WITH AND PHOSPHORYLATED BY THE TYPE-II TGF-BETA RECEPTOR [J].
CHEN, RH ;
MIETTINEN, PJ ;
MARUOKA, EM ;
CHOY, L ;
DERYNCK, R .
NATURE, 1995, 377 (6549) :548-552
[8]   Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant and defective in a glycogen synthase kinase 3β-like kinase [J].
Choe, S ;
Schmitz, RJ ;
Fujioka, S ;
Takatsuto, S ;
Lee, MO ;
Yoshida, S ;
Feldmann, KA ;
Tax, FE .
PLANT PHYSIOLOGY, 2002, 130 (03) :1506-1515
[9]   The type II transforming growth factor (TGF)-β receptor-interacting protein TRIP-1 acts as a modulator of the TGF-β response [J].
Choy, L ;
Derynck, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (47) :31455-31462
[10]   Brassinosteroid signal transduction: Clarifying the pathway from ligand perception to gene expression [J].
Clouse, SD .
MOLECULAR CELL, 2002, 10 (05) :973-982