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Specifying the role of BAK1‐interacting receptor‐like kinase 3 in brassinosteroid signaling
Journal of Integrative Plant Biology ( IF 9.3 ) Pub Date : 2019-06-11 , DOI: 10.1111/jipb.12803 Ruth Großeholz 1 , Anna Feldman‐Salit 1 , Friederike Wanke 2 , Sarina Schulze 2 , Nina Glöckner 2 , Birgit Kemmerling 2 , Klaus Harter 2 , Ursula Kummer 1
Journal of Integrative Plant Biology ( IF 9.3 ) Pub Date : 2019-06-11 , DOI: 10.1111/jipb.12803 Ruth Großeholz 1 , Anna Feldman‐Salit 1 , Friederike Wanke 2 , Sarina Schulze 2 , Nina Glöckner 2 , Birgit Kemmerling 2 , Klaus Harter 2 , Ursula Kummer 1
Affiliation
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Brassinosteroids (BR) are involved in the control of several developmental processes ranging from root elongation to senescence and adaptation to environmental cues. Thus, BR perception and signaling have to be precisely regulated. One regulator is BRI1‐associated kinase 1 (BAK1)‐interacting receptor‐like kinase 3 (BIR3). In the absence of BR, BIR3 forms complexes with BR insensitive 1 (BRI1) and BAK1. However, the biophysical and energetic requirements for complex formation in the absence of the ligand have yet to be determined. Using computational modeling, we simulated the potential complexes between the cytoplasmic domains of BAK1, BRI1 and BIR3. Our calculations and experimental data confirm the interaction of BIR3 with BAK1 and BRI1, with the BAK1 BIR3 interaction clearly favored. Furthermore, we demonstrate that BIR3 and BRI1 share the same interaction site with BAK1. This suggests a competition between BIR3 and BRI1 for binding to BAK1, which results in preferential binding of BIR3 to BAK1 in the absence of the ligand thereby preventing the active participation of BAK1 in BR signaling. Our model also suggests that BAK1 and BRI1 can interact even while BAK1 is in complex with BIR3 at an additional binding site of BAK1 that does not allow active BR signaling.
中文翻译：
明确BAK1相互作用受体样激酶3在油菜素类固醇信号传导中的作用
油菜素类固醇（BR）参与了从根部延伸到衰老以及对环境线索的适应等几个发育过程的控制。因此，必须精确地调节BR的感知和信令。一种调节剂是与BRI1相关的激酶1（BAK1）相互作用的受体样激酶3（BIR3）。在不存在BR的情况下，BIR3与BR不敏感1（BRI1）和BAK1形成复合物。然而，在没有配体的情况下，对于复合物形成的生物物理和能量需求尚未确定。使用计算模型，我们模拟了BAK1，BRI1和BIR3的胞质域之间的潜在复合物。我们的计算和实验数据证实了BIR3与BAK1和BRI1的相互作用，其中BAK1与BIR3的相互作用显然受到青睐。此外，我们证明BIR3和BRI1与BAK1共享相同的相互作用位点。这表明BIR3和BRI1之间竞争与BAK1的结合，这导致在不存在配体的情况下BIR3与BAK1优先结合，从而阻止了BAK1主动参与BR信号传导。我们的模型还表明，即使BAK1与BIR3处于复杂的BAK1结合位点，BAK1和BRI1也可以相互作用，而BAK1的其他结合位点不允许活性BR信号传导。
更新日期：2019-06-11
中文翻译：
明确BAK1相互作用受体样激酶3在油菜素类固醇信号传导中的作用
油菜素类固醇（BR）参与了从根部延伸到衰老以及对环境线索的适应等几个发育过程的控制。因此，必须精确地调节BR的感知和信令。一种调节剂是与BRI1相关的激酶1（BAK1）相互作用的受体样激酶3（BIR3）。在不存在BR的情况下，BIR3与BR不敏感1（BRI1）和BAK1形成复合物。然而，在没有配体的情况下，对于复合物形成的生物物理和能量需求尚未确定。使用计算模型，我们模拟了BAK1，BRI1和BIR3的胞质域之间的潜在复合物。我们的计算和实验数据证实了BIR3与BAK1和BRI1的相互作用，其中BAK1与BIR3的相互作用显然受到青睐。此外，我们证明BIR3和BRI1与BAK1共享相同的相互作用位点。这表明BIR3和BRI1之间竞争与BAK1的结合，这导致在不存在配体的情况下BIR3与BAK1优先结合，从而阻止了BAK1主动参与BR信号传导。我们的模型还表明，即使BAK1与BIR3处于复杂的BAK1结合位点，BAK1和BRI1也可以相互作用，而BAK1的其他结合位点不允许活性BR信号传导。
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