Hyeong-jun Han, Bu Young Choi and Young-Joon Surh* Pages 4422 - 4425 ( 4 )
Pin1 is a unique peptidyl-prolyl cis/trans isomerase (PPIase) that catalyzes the cis/trans isomerization of peptidyl-prolyl peptide bonds of its substrate proteins by binding to their specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. This alters the conformation of target proteins and consequently affects their stability, intracellular localization, and/or biological functions. The abnormal overexpression of Pin1 is observed in some malignancies, which is associated with cancer cell proliferation, migration and invasion. However, a role for Pin1 as a putative tumor suppressor has recently been suggested. Systematic dissection of pro-oncogenic vs. tumor suppressive functions of Pin1 will be necessary.
Pin1, proline-directed protein kinases, phosphorylation-dependent peptidyl-prolyl isomerase, pSer/Thr-Pro motif, PPIase, proline isomerization.
Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 08826, Department of Pharmaceutical Science and Engineering, School of Convergence Bioscience and Technology, Seowon University, Chungbuk, Tumor Microenvironment Global Core Research Center, College of Pharmacy, Seoul National University, Seoul 08826