Study discovered SOBIR1/EVR as a regulator of secondary growth. SOBIR1/EVR acts through a mechanism that involves BREVIPEDICELLUS (BP) and ERECTA (ER). SOBIR1/EVR physically interacts with ER and that defects caused by the sobir1/evr mutation are aggravated by mutating ER indicating that SOBIR1/EVR and ERECTA act together in the control of the precocious formation of xylem fiber development.
The 1.55 A resolution crystal structure of the immune receptor kinase SOBIR1 from Arabidopsis is presented. The ectodomain structure reveals the presence of five leucine-rich repeats sandwiched between noncanonical capping domains. The disulfide-bond-stabilized N-terminal cap harbours an unusual beta-hairpin structure.
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