Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1.

Abstract:

:Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation.

journal_name

Cell Res

journal_title

Cell research

authors

Wang J,Jiang J,Wang J,Chen L,Fan SL,Wu JW,Wang X,Wang ZX

doi

10.1038/cr.2014.132

subject

Has Abstract

pub_date

2014-11-01 00:00:00

pages

1328-41

issue

11

eissn

1001-0602

issn

1748-7838

pii

cr2014132

journal_volume

24

pub_type

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