Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1)receptor kinase by autophosphorylation within the glycine-rich loop (Record no. 48008)

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fixed length control field 02526nam a2200253Ia 4500
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control field MX-MdCICY
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control field 20250625153929.0
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Transcribing agency CICY
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Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-13811
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Title Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1)receptor kinase by autophosphorylation within the glycine-rich loop
490 0# - SERIES STATEMENT
Volume/sequential designation PNAS, 109(1), p.327-332, 2012
520 3# - SUMMARY, ETC.
Summary, etc. The 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.
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Topical term or geographic name entry element PHOSPHOTYROSINE
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Topical term or geographic name entry element SIGNAL TRANSDUCTION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHOSPHOSERINE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element MODIFICATIONSPECIFIC ANTIBODIES
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Oh, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Wang, X.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Clouse, S.D.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Huber, S.C.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1KWFSFZ23_4fWdpltf_OwLW9me3U-kvmy/view?usp=drivesdk">https://drive.google.com/file/d/1KWFSFZ23_4fWdpltf_OwLW9me3U-kvmy/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-13811 25.06.2025 25.06.2025 Documentos solicitados