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(email: hlee1971@bcpl.net)

Reversible protein phosphorylation is a regulatory mechanism playing a central role in signal transduction pathways. We are investigating the role of protein phosphorylation in controlling intercellular signaling. We have biochemically isolated a member of the Casein Kinase I family as a putative kinase that is targeted to plasmodesmata and might be involved in targeting (and/or trafficking) of macromolecules. This kinase is named PAPK for plasmodesmal-associated protein kinase. Currently, we are focusing on understanding the molecular mechanism underlying the intracellular targeting of an Arabidopsis isoform, PAPK1 and its biological function in the context of developmental cell patterning, and cell-to-cell communication.

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