期刊
EXPERIMENTAL CELL RESEARCH
卷 335, 期 1, 页码 115-122出版社
ELSEVIER INC
DOI: 10.1016/j.yexcr.2015.04.019
关键词
Podoplanin; Serine phosphorylation; Protein Kinase A; Cyclin dependent Kinase 5; Cell migration
资金
- Foundation of UMDNJ
- Osteopathic Heritage Foundation
- Northarvest Bean Growers Association
- National Institutes of Health [R01 CA 58530, HL 083034]
- NIH [046593]
Podoplanin (PDPN) is a transmembrane glycoprotein that promotes tumor cell migration, invasion, and cancer metastasis. In fact, PDPN expression is induced in many types of cancer. Thus, PDPN has emerged as a functionally relevant cancer biomarker and chemotherapeutic target. PDPN contains 2 intracellular serine residues that are conserved between species ranging from mouse to humans. Recent studies indicate that protein kinase A (PKA) can phosphorylate PDPN in order to inhibit cell migration. However, the number and identification of specific residues phosphorylated by PICA have not been defined. In addition, roles of other kinases that may phosphorylate PDPN to control cell migration have not been investigated. We report here that cyclin dependent kinase 5 (CDK5) can phosphorylate PDPN in addition to PICA. Moreover, results from this study indicate that PICA and CDK5 cooperate to phosphorylate PDPN on both intracellular serine residues to decrease cell motility. These results provide new insight into PDPN phosphorylation dynamics and the role of PDPN in cell motility. Understanding novel mechanisms of PDPN intracellular signaling could assist with designing novel targeted chemotherapeutic agents and procedures. (C) 2015 Elsevier Inc. All rights reserved.
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