Paper Report for: Li_2001_Proc.Natl.Acad.Sci.U.S.A_98_5916
Reference
Title: BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana Li J, Lease KA, Tax FE, Walker JC Ref: Proc Natl Acad Sci U S A, 98:5916, 2001 : PubMed
Brassinosteroid-insensitive 1 (BRI1) of Arabidopsis thaliana encodes a cell surface receptor for brassinosteroids. Mutations in BRI1 severely affect plant growth and development. Activation tagging of a weak bri1 allele (bri1-5) resulted in the identification of a new locus, brs1-1D. BRS1 is predicted to encode a secreted carboxypeptidase. Whereas a brs1 loss-of-function allele has no obvious mutant phenotype, overexpression of BRS1 can suppress bri1 extracellular domain mutants. Genetic analyses showed that brassinosteroids and a functional BRI1 protein kinase domain are required for suppression. In addition, overexpressed BRS1 missense mutants, predicted to abolish BRS1 protease activity, failed to suppress bri1-5. Finally, the effects of BRS1 are selective: overexpression in either wild-type or two other receptor kinase mutants resulted in no phenotypic alterations. These results strongly suggest that BRS1 processes a protein involved in an early event in the BRI1 signaling.
Li J, Lease KA, Tax FE, Walker JC (2001) BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana Proc Natl Acad Sci U S A98: 5916-21
Li J, Lease KA, Tax FE, Walker JC (2001) Proc Natl Acad Sci U S A98: 5916-21