Abstract
The serine/threonine kinase homeodomain-interacting protein kinase (HIPK2) is a tumor suppressor and functions as an evolutionary conserved regulator of signaling and gene expression. This kinase regulates a surprisingly vast array of biological processes that range from the DNA damage response and apoptosis to hypoxia signaling and cell proliferation. Recent studies show the tight control of HIPK2 by hierarchically occurring posttranslational modifications such as phosphorylation, small ubiquitin-like modifier modification, acetylation, and ubiquitination. The physiological function of HIPK2 as a regulator of cell proliferation and survival has a downside: proliferative diseases. Dysregulation of HIPK2 can result in increased proliferation of cell populations as it occurs in cancer or fibrosis. We discuss various models that could explain how inappropriate expression, modification, or localization of HIPK2 can be a driver for these proliferative diseases.
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Acknowledgments
This work was supported by grants from the German Research Foundation projects SCHM 1417/4-2, SCHM 1417/7-1, SCHM 1417/8-1, GRK 1566/1, SFB/TRR 81, the Excellence Cluster Cardio-Pulmonary System (ECCPS), German Academic Exchange Service (A/08/98404) and the LOEWE/UGMLC program.
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Saul, V.V., Schmitz, M.L. Posttranslational modifications regulate HIPK2, a driver of proliferative diseases. J Mol Med 91, 1051–1058 (2013). https://doi.org/10.1007/s00109-013-1042-0
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DOI: https://doi.org/10.1007/s00109-013-1042-0