Protein Kinases and Associated Pathways in Pluripotent State and Lineage Differentiation
Melina Shoni, Kathy O. Lui, Demetrios G. Vavvas, Michael G. Muto, Ross S. Berkowitz, Nikolaos Vlahos and Shu-Wing Ng
Pages 366-387 (22)
Protein kinases (PKs) mediate the reversible conversion of substrate proteins to phosphorylated forms, a key
process in controlling intracellular signaling transduction cascades. Pluripotency is, among others, characterized by specifically
expressed PKs forming a highly interconnected regulatory network that culminates in a finely-balanced molecular
switch. Current high-throughput phosphoproteomic approaches have shed light on the specific regulatory PKs and their
function in controlling pluripotent states. Pluripotent cell-derived endothelial and hematopoietic developments represent
an example of the importance of pluripotency in cancer therapeutics and organ regeneration. This review attempts to provide
the hitherto known kinome profile and the individual characterization of PK-related pathways that regulate pluripotency.
Elucidating the underlying intrinsic and extrinsic signals may improve our understanding of the different pluripotent
states, the maintenance or induction of pluripotency, and the ability to tailor lineage differentiation, with a particular
focus on endothelial cell differentiation for anti-cancer treatment, cell-based tissue engineering, and regenerative medicine
Endothelial cells, phosphorylation, pluripotency, protein kinases, signaling pathways, stem cell.
221 Longwood Avenue, BLI- 449A, Boston MA 02115, USA.