Journal
GENES & DEVELOPMENT
Volume 25, Issue 3, Pages 232-237Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.2001911
Keywords
tyrosine phosphorylation; linear motif; plant receptor kinase; brassinosteroid signaling
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Funding
- European Molecular Biology Organization
- International Human Frontier Science Program Organization
- Life Sciences Research Foundation
- Marc and Eva Stern Foundation
- Howard Hughes Medical Institute
- National Science Foundation [IOS-0649389]
- National Institutes of Health [1 R01 GM086639]
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Receptor tyrosine kinases control many critical processes in metazoans, but these enzymes appear to be absent in plants. Recently, two Arabidopsis receptor kinases-BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1), the receptor and coreceptor for brassinosteroids-were shown to autophosphorylate on tyrosines. However, the cellular roles for tyrosine phosphorylation in plants remain poorly understood. Here, we report that the BRI1 KINASE INHIBITOR 1 (BKI1) is tyrosine phosphorylated in response to brassinosteroid perception. Phosphorylation occurs within a reiterated [KR][KR] membrane targeting motif, releasing BKI1 into the cytosol and enabling formation of an active signaling complex. Our work reveals that tyrosine phosphorylation is a conserved mechanism controlling protein localization in all higher organisms.
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