Sandbox Reserved 935: Difference between revisions
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<scene name='57/579705/4oab/1'>Testi3</scene> | <scene name='57/579705/4oab/1'>Testi3</scene> | ||
==Introduction== | ==Introduction== | ||
Brassinosteroid insensitive 1 (BRI1) is a membrane receptor that senses brassinosteroides, which are polyhydroxylated steroid hormones <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain | Brassinosteroid insensitive 1 (BRI1) is a membrane receptor that senses brassinosteroides, which are polyhydroxylated steroid hormones <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. Brassinosteroids control planth growth and development by activating BRI1 and starting a signaling pathway that leads to nuclear thanscription factors being activated. BRI1 is thought to be a dual-specificity kinase and it has structural features reminiscent of both serine/threonine and tyrosine kinases. | ||
and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. Brassinosteroids control planth growth and development by activating BRI1 and starting a signaling pathway that leads to nuclear thanscription factors being activated. BRI1 is thought to be a dual-specificity kinase and it has structural features reminiscent of both serine/threonine and tyrosine kinases. | |||
In the cell, BRI1 cycles between the plasma membrane and endosomes <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. When not activated, BRI1 is auto-inhibited by its own C-terminal tail as well as auto-phosphorylation of Thr872 and interaction with BRI1 kinase inhibitor protein BKI1 in the kinase domain. BKI1 also contains an N-terminal targeting motif for the plasma membrane. When the extracellular LRR domain gets activated by a brassinosteroid, it causes a reordering of 70 residues and creates a docking platform for the co-receptor SERK (somatic embryogenesis receptor kinase). The C-termini of BRI1 and SERK trans-phosphorylate each other, releasing the BKI1 from BRI1 and allowing BRI1 to phosphorylate immediate downstream signaling components (such as BRI1 substrate kinases, or BSKs). | In the cell, BRI1 cycles between the plasma membrane and endosomes <ref>Daniel Bojar, Jacobo Martinez, Julia Santiago, Vladimir Rybin, Richard Bayliss and Michael Hothorn: Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation. The Plant Journal (2014) 78, 31–43. PMID: 24461462 doi: 10.1111/tpj.12445</ref>. When not activated, BRI1 is auto-inhibited by its own C-terminal tail as well as auto-phosphorylation of Thr872 and interaction with BRI1 kinase inhibitor protein BKI1 in the kinase domain. BKI1 also contains an N-terminal targeting motif for the plasma membrane. When the extracellular LRR domain gets activated by a brassinosteroid, it causes a reordering of 70 residues and creates a docking platform for the co-receptor SERK (somatic embryogenesis receptor kinase). The C-termini of BRI1 and SERK trans-phosphorylate each other, releasing the BKI1 from BRI1 and allowing BRI1 to phosphorylate immediate downstream signaling components (such as BRI1 substrate kinases, or BSKs). | ||
