Prolyl isomerase Pin1 in cancer  

作　　者：Zhimin LU Tony Hunter 

机构地区：[1]Brain Tumor Center and Department of Neuro-Oncology [2]Department of Molecular and Cellular Oncology [3]Cancer Biology Program, The University of Texas Graduate School of Biomedical Sciences at Houston, Houston, TX 77030, USA [4]Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 9203 7, USA

出　　处：《Cell Research》2014年第9期1033-1049,共17页细胞研究（英文版）

摘　　要：Proline-directed phosphorylation is a posttranslational modification that is instrumental in regulating signaling from the plasma membrane to the nucleus, and its dysregulation contributes to cancer development. Protein interacting with never in mitosis A1 （Pinl）, which is overexpressed in many types of cancer, isomerizes specific phosphorylat- ed Ser/Thr-Pro bonds in many substrate proteins, including glycolytic enzyme, protein kinases, protein phosphatases, methyltransferase, lipid kinase, ubiquitin E3 ligase, DNA endonuclease, RNA polymerase, and transcription activa- tors and regulators. This Pinl-mediated isomerization alters the structures and activities of these proteins, thereby regulating cell metabolism, cell mobility, cell cycle progression, cell proliferation, cell survival, apoptosis and tumor development.

关 键 词：PINL PHOSPHORYLATION CANCER 

分 类 号：Q558.03[生物学—生物化学] X503.1[环境科学与工程—环境工程]