Award Abstract # 0132554
Novel Components of Brassinosteroid Signaling

NSF Org: IOS
Division Of Integrative Organismal Systems
Recipient: UNIVERSITY OF MISSOURI SYSTEM
Initial Amendment Date: January 3, 2002
Latest Amendment Date: January 3, 2002
Award Number: 0132554
Award Instrument: Continuing Grant
Program Manager: Stephen Herbert
IOS
 Division Of Integrative Organismal Systems
BIO
 Directorate for Biological Sciences
Start Date: February 1, 2002
End Date: September 30, 2002 (Estimated)
Total Intended Award Amount: $383,350.00
Total Awarded Amount to Date: $143,350.00
Funds Obligated to Date: FY 2002 = $59,027.00
History of Investigator:
  • Jia Li (Principal Investigator)
    lij@ou.edu
  • John Walker (Co-Principal Investigator)
Recipient Sponsored Research Office: University of Missouri-Columbia
121 UNIVERSITY HALL
COLUMBIA
MO  US  65211-3020
(573)882-7560
Sponsor Congressional District: 03
Primary Place of Performance: University of Missouri-Columbia
121 UNIVERSITY HALL
COLUMBIA
MO  US  65211-3020
Primary Place of Performance
Congressional District:
03
Unique Entity Identifier (UEI): SZPJL5ZRCLF4
Parent UEI:
NSF Program(s): INSTRUMENTAT & INSTRUMENT DEVP,
SIGNAL TRANSDCTN/CELL REGULATN,
INTEGRATIVE PLANT BIOLOGY
Primary Program Source: app-0102 
app-0103 

app-0104 
Program Reference Code(s): 1108, 1136, 1145, 9109, BIOT
Program Element Code(s): 110800, 113600, 114500
Award Agency Code: 4900
Fund Agency Code: 4900
Assistance Listing Number(s): 47.074

ABSTRACT

Brassinosteroids are plant hormones that perform a fundamental role in coordinating growth and development. The Arabidopsis gene, Brassinosteroid Insensitive 1 (BRI1), encodes a receptor-like protein kinase (RLK), which is a critical component in brassinosteroid-mediated signaling. Using activation tagging, we identified a gene can suppress the growth defects of a mutant bri1 allele. This bri1 suppressor, BRS1, is predicted to encode a secreted serine carboxypeptidase. Elevated expression of BRS1 suppresses two bri1 alleles that have mutations in their extracellular domain, but not a kinase domain mutation. Genetic and physiological data strongly suggest BRS1 regulates an early step in brassinosteroid signaling. In many signal transduction pathways proteolytic processing plays an important role in regulating signal perception and transduction. We hypothesize that BRS1 is involved in a proteolytic processing step in the BRI1 signaling pathway. To test this hypothesis, we propose to undertake a detailed characterization of BRS1, including its cellular and subcellular localization, and analysis of its enzymatic activity. In addition, BRS1 is a member of a gene family. To examine a possible involvement of BRS1 and the BRS1-like genes in BRI1 and other RLK signaling pathways, we will use genetic approaches to investigate their function. These studies will contribute to our understanding of brassinosteroid signaling and other RLK mediated processes that control growth and development in plants.

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