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245 1 0 _aDeactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1)receptor kinase by autophosphorylation within the glycine-rich loop
490 0 _vPNAS, 109(1), p.327-332, 2012
520 3 _aThe activity of the dual-specificity receptor kinase, brassinosteroid insensitive 1 (BRI1), reflects the balance between phosphorylationdependent activation and several potential mechanisms for deactivation of the receptor. In the present report, we elucidate a unique mechanism for deactivation that involves autophosphorylation of serine-891 in the ATP-binding domain. Serine-891 was identified previously as a potential site of autophosphorylation by mass spectrometry, and sequence-specific antibodies and mutagenesis studies now unambiguously establish phosphorylation of this residue. In vivo, phosphorylation of serine-891 increased slowly with time following application of brassinolide (BL)to Arabidopsis seedlings, whereas phosphorylation of threonine residues increased rapidly and then remained constant. Transgenic plants expressing the BRI1(S891A)-Flag-directed mutant have increased hypocotyl and petiole lengths, relative to wild-type BRI1- Flag (both in the bri1-5 background), and accumulate higher levels of the unphosphorylated form of the BES1 transcription factor in response to exogenous BL. In contrast, plants expressing the phosphomimetic S891D-directed mutant are severely dwarfed and do not accumulate unphosphorylated BES1 in response to BL. Collectively, these results suggest that autophosphorylation of serine-891 is one of the deactivation mechanisms that inhibit BRI1 activity and BR signaling in vivo. Many arginine-aspartate (RD)-type leucine- rich repeat receptor-like kinases have a phosphorylatable residue within the ATP-binding domain, suggesting that this mechanism may play a broad role in receptor kinase deactivation.
650 1 4 _aPHOSPHOTYROSINE
650 1 4 _aSIGNAL TRANSDUCTION
650 1 4 _aPHOSPHOSERINE
650 1 4 _aMODIFICATIONSPECIFIC ANTIBODIES
700 1 2 _aOh, M.
700 1 2 _aWang, X.
700 1 2 _aClouse, S.D.
700 1 2 _aHuber, S.C.
856 4 0 _uhttps://drive.google.com/file/d/1KWFSFZ23_4fWdpltf_OwLW9me3U-kvmy/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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