Steroid hormones are crucial for embryonic development and adult homeostasis in animals. Brassinosteroids (BRs), a special class of plant steroids, have pronounced growth-promoting effects on plants when applied exogenously. Recent genetic studies on dwarf mutants of Arabidopsis, pea, and tomato have confirmed that BRs are important plant hormones that are essential for normal plant growth. Molecular and genetic approaches have been taken to dissect the BR signal transduction pathway, leading to the identification of a few BR-regulated genes and the Arabidopsis BRI1 gene encoding a putative BR receptor. However, the signaling events between BRI1 and various BR-induced cellular responses remains unknown. To understand how BRs are perceived on cell surface and transmitted into cells to regulate many cellular responses, a combination of biochemical, molecular, and genetic approaches will be used to identify additional components of the BR signaling cascade with the following 5 specific aims: (l) Further characterize specific BRI1-interacting proteins identified through a yeast two-hybrid screen and determine the biological and biochemical functions of the most promising BRI1 interactors. (2) Clone the second Arabidopsis BR-insensitive locus, BIN2, and examine its role in BR signaling. (3) Conduct a large-scale genetic interaction screen to identify BR signaling components whose mutations can modify the det2 (a weak BR-deficient mutant) phenotype. (4) Clone at least one of the det2 modifier genes. (5) Perform other genetic screens to identify novel BR signaling mutants. Results of these proposed studies will provide insights into the molecular mechanism(s) by which BRs regulate plant growth and development, thus enhancing our ability to genetically manipulate plant growth to improve crop quality and productivity. in addition, by identifying genes involved in the plant steroid signal transduction, it may be possible to discover previously unidentified signaling components involved in membrane- initiated animal steroid signaling, thereby adding new knowledge to our general understanding of steroid hormone actions and ultimately leading to the identification of more and better targets for treating human diseases.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM060519-04
Application #
6627278
Study Section
Genetics Study Section (GEN)
Program Officer
Anderson, James J
Project Start
2000-01-01
Project End
2004-12-31
Budget Start
2003-01-01
Budget End
2003-12-31
Support Year
4
Fiscal Year
2003
Total Cost
$225,319
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
073133571
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Liu, Yidan; Li, Jianming (2013) A conserved basic residue cluster is essential for the protein quality control function of the Arabidopsis calreticulin 3. Plant Signal Behav 8:e23864
Liu, Yidan; Li, Jianming (2013) An in vivo investigation of amino acid residues critical for the lectin function of Arabidopsis calreticulin 3. Mol Plant 6:985-7
Su, Wei; Liu, Yidan; Xia, Yang et al. (2012) The Arabidopsis homolog of the mammalian OS-9 protein plays a key role in the endoplasmic reticulum-associated degradation of misfolded receptor-like kinases. Mol Plant 5:929-40
Hong, Zhi; Kajiura, Hiroyuki; Su, Wei et al. (2012) Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis. Proc Natl Acad Sci U S A 109:11437-42
Li, Jianming (2011) Direct involvement of leucine-rich repeats in assembling ligand-triggered receptor-coreceptor complexes. Proc Natl Acad Sci U S A 108:8073-4
Shang, Yun; Lee, Myeong Min; Li, Jianming et al. (2011) Characterization of cp3 reveals a new bri1 allele, bri1-120, and the importance of the LRR domain of BRI1 mediating BR signaling. BMC Plant Biol 11:8
Su, Wei; Liu, Yidan; Xia, Yang et al. (2011) Conserved endoplasmic reticulum-associated degradation system to eliminate mutated receptor-like kinases in Arabidopsis. Proc Natl Acad Sci U S A 108:870-5
Kang, Bin; Wang, Hao; Nam, Kyoung Hee et al. (2010) Activation-tagged suppressors of a weak brassinosteroid receptor mutant. Mol Plant 3:260-8
Peng, Peng; Zhao, Jun; Zhu, Yongyou et al. (2010) A direct docking mechanism for a plant GSK3-like kinase to phosphorylate its substrates. J Biol Chem 285:24646-53
Li, Jianming (2010) Regulation of the nuclear activities of brassinosteroid signaling. Curr Opin Plant Biol 13:540-7

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