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Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor.

ABSTRACT: 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.

SUBMITTER: Jaillais Y

PROVIDER: S-EPMC3034898 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor.

Jaillais Yvon Y Hothorn Michael M Belkhadir Youssef Y Dabi Tsegaye T Nimchuk Zachary L ZL Meyerowitz Elliot M EM Chory Joanne J

Genes & development 20110201 3

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 phosp ...[more]

PMID: 21289069

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