| Literature DB >> 28671058 |
Hyeong-Jun Han1, Bu Young Choi2, Young-Joon Surh1.
Abstract
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. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.org.Entities:
Keywords: PPIase; Pin1; pSer/Thr-Pro motif; phosphorylation-dependent peptidyl-prolyl isomerase; prolinezzm321990isomerization; proline-directed protein kinases
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Year: 2017 PMID: 28671058 DOI: 10.2174/1381612823666170703164711
Source DB: PubMed Journal: Curr Pharm Des ISSN: 1381-6128 Impact factor: 3.116