IndraLab

Statements


| 3

sparser
"It indicates that ZAR1’s auto-phosphorylation is promoted by the binding of CaM1 or AGB1, but the binding is independent on the ZAR1 kinase activity, as CaM1 or AGB1 interacts with His-kinase K534>A . These data, together, strongly suggest that ZAR1, AGB1 and CaM1 form complex and the ZAR1 kinase activity is activated by the binding of CaM1 and/or AGB1."

sparser
"These data suggest that ZAR1 may act as a membrane receptor kinase to form a complex with CaM1 and AGB1, to activate corresponding signaling cascades that modulate the asymmetric division of the zygote."

sparser
"To further investigate whether the binding of CaM1 and AGB1 affects ZAR1 kinase activity, in vitro pull-down experiment was performed."