IndraLab

Statements


| 3

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

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."