• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the glycine-rich loop
【24h】

Deactivation of the Arabidopsis BRASSINOSTEROID INSENSITIVE 1 (BRI1) receptor kinase by autophosphorylation within the glycine-rich loop

机译：富含甘氨酸的环内的自磷酸化使拟南芥菜核固醇不敏感1（BRI1）受体激酶失活

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The activity of the dual-specificity receptor kinase, brassinosteroid insensitive 1 (BRI1), reflects the balance between phosphorylation-dependent 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 muta-genesis 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 phos-phomimetic 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 leu-cine-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.
机译：双特异性受体激酶，油菜素甾体不敏感1（BRI1）的活性反映了磷酸化依赖性激活与该受体失活的几种潜在机制之间的平衡。在本报告中，我们阐明了一种独特的失活机制，该机制涉及在ATP结合域中丝氨酸891的自磷酸化。丝氨酸891先前已通过质谱鉴定为潜在的自磷酸化位点，而序列特异性抗体和诱变研究现已明确确定该残基的磷酸化。在体内，将油菜素内酯（BL）应用于拟南芥幼苗后，丝氨酸891的磷酸化随时间缓慢增加，而苏氨酸残基的磷酸化迅速增加，然后保持恒定。相对于野生型BRI1-Flag（均在bri1-5背景中），表达BRI1（S891A）-Flag定向突变体的转基因植物的胚轴和叶柄长度增加，并且积累了更高水平的BES1转录的非磷酸化形式相对于外源BL的响应因子，与之相反，表达抗拟磷酸S891D定向突变体的植物严重矮化，并且不积累对BL响应的未磷酸化BES1。总的来说，这些结果表明丝氨酸891的自磷酸化是在体内抑制BRI1活性和BR信号传导的失活机制之一。许多精氨酸-天冬氨酸（RD）型富含亮氨酸的重复受体样激酶在ATP结合域内具有可磷酸化的残基，表明该机制可能在受体激酶失活中发挥广泛作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号