期刊
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY
卷 8, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2020.00120
关键词
cancer therapeutics; PIN1; PIN1 inhibitor; proline-directed phosphorylation; prolyl isomerase; tumorigenesis
资金
- National Research Foundation of Korea (NRF) - Korean Government [NRF-2015M3A9C7030181, NRF-2016M3A9E4947797, NRF-2017R1D1A1B03034810]
- National Research Foundation of Korea [2015M3A9C7030181] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Peptidyl-prolyl isomerase (PIN1) specifically binds and isomerizes the phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif, which results in the alteration of protein structure, function, and stability. The altered structure and function of these phosphorylated proteins regulated by PIN1 are closely related to cancer development. PIN1 is highly expressed in human cancers and promotes cancer as well as cancer stem cells by breaking the balance of oncogenes and tumor suppressors. In this review, we discuss the roles of PIN1 in cancer and PIN1-targeted small-molecule compounds.
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